CN101180431A - 纤维基质表面的涂布 - Google Patents
纤维基质表面的涂布 Download PDFInfo
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Abstract
本发明涉及使用至少一种疏水蛋白涂布选自织物或皮革基质的纤维基质的方法。
Description
技术领域
本发明系涉及一种藉由使用至少一种疏水蛋白来涂布选自织物基质及皮革之纤维基质表面的方法。本发明进一步涉及选自织物基质及皮革之经涂布纤维基质，还涉及使用本发明之纤维基质生产服装之方法。
背景技术
WO 02/59413揭示使用蛋白质或多肽处理织物，例如聚酯、聚丙烯酸、聚酰胺，尤其是溶于水之经氧化羊毛，以便在使用时具有绒状手感。但常见情形系：按照WO 02/59413制成的织物开始会具有一极为令人不悦之手感。亦观察到藉由一步方法达成均匀应用可能较为困难(原文第10页)。为避免在达成均匀应用方面之此困难，有人提出利用氯甲代氧丙环的极为复杂的多步骤方法作为补救方案。然而，一般不期望使用氯甲代氧丙环。
发明内容
本发明之一目的系提供一种可避免现有技术之缺点的方法。
我们已发现：此目的可藉由在本文开篇处所界定之方法达成。
开篇处所界定之方法开始于一或多个表面，该表面可为平滑的或有纹理的。拟涂布之表面形成选自织物基质及皮革之纤维基质的一部分。
具体实施方式
对于本发明而言，织物基质系织物纤维、织物中间品以及自该等制造之最终产品及成品，以及用于服装工业之织物；且亦包括(例如)地毯及其它家用织物以及工业用织物结构。这些包括未成型结构(例如纤维)、线性结构(例如麻线、长丝、纱线、长麻、并丝、花边、辫带、绳索)以及三维结构(例如毛毡、织布、成形针织圈、无纺织物及填絮)。织物基质可为天然材料，如棉花、羊毛或亚麻、或与例如棉花/聚酯、棉花/聚酰胺之掺合物。对于本发明而言，织物优选为聚丙烯腈、聚酰胺且尤其为聚酯、或天然材料与聚丙烯腈、聚酰胺且尤其与聚酯之掺合物。
对于本发明而言，皮革优选指鞣制及成品动物兽皮且亦指所谓的剖层皮。
对于本发明而言，涂层系指覆盖欲按照本发明涂布的基质面积之至少10％，优选至少25％且更优选至少50％的至少一种疏水蛋白之单分子层。纤维基质之覆盖程度可藉由常规方法(例如，显微镜方法)测定。
本发明利用至少一种疏水蛋白来涂布纤维基质之表面。可使用一种疏水蛋白或多数种不同疏水蛋白之混合物。
疏水蛋白系为丝状真菌(例如裂褶菌(Schizophyllum commune))所特有之熟知蛋白质，优选为小肽。它们一般具有8个半胱氨酸单元。疏水蛋白可与天然来源分离。但亦可能藉由化学及/或生物技术生产方法合成非天然疏水蛋白。
本文所用术语“疏水蛋白”优选应指具有结构通式(I)之蛋白质：
Xn-C1-X1-50-C2-X0-5-C3-X1-100-C4-X1-100-C5-X1-50-C6-X0-5-C7-X1-50-C8-Xm
(I)
其中X可以是20种天然存在的氨基酸(Phe，Leu，Ser，Tyr，Cys，Trp，Pro，His，Gln，Arg，Ile，Met，Thr，Asn，Lys，Val，Ala，Asp，Glu，Gly)的任一种。每个X可以是相同或不同的。X旁的下标都是氨基酸数目，C代表半胱氨酸、丙氨酸、丝氨酸、甘氨酸、甲硫氨酸或者苏氨酸，条件是用C表示的至少四个氨基酸是半胱氨酸，并且下标n和m各自独立地是0到500，优选15到300之间的自然数。
本发明之一个实施方案利用在涂布于一玻璃表面上后具有以下特性之疏水蛋白：与未经涂布玻璃表面上同样尺寸水滴所形成的接触角相比，该疏水蛋白可使水滴(5微升)之接触角增加至少20°、优选至少25°且更优选30°，每一测量皆于室温下实施。
用C1到C8表示的氨基酸优选为半胱氨酸；然而，它们还可以用具有相似体积的其他氨基酸替换，优选用丙氨酸、丝氨酸、苏氨酸、甲硫氨酸或者甘氨酸替换。然而，C1到C8位的至少4个，优选至少5个，更优选至少6个，尤其至少7个位置应该由半胱氨酸组成。在本发明蛋白质中，半胱氨酸可以以还原的形式存在或者相互形成二硫桥。尤其优选分子内形成C-C桥，特别具有至少一个分子内二硫桥，优选2个，更优选3个，最优选4个分子内二硫桥。对于上述半胱氨酸用具有相似体积的氨基酸交换的情况，此类C位置有利地成对交换，其可以相互形成分子内二硫桥。
当在称作X的位置中使用半胱氨酸、丝氨酸、丙氨酸、甘氨酸、甲硫氨酸或者苏氨酸时，可以对应地改变通式中各个C位置的编号。
优选使用通式(II)的疏水蛋白：
Xn-C1-X3-25-C2-X0-2-C3-X5-50-C4-X2-35-C5-X2-15-C6-X0-2-C7-X3-35-C8-Xm
(II)
其中X，C和X和C旁的下标每个如上定义，下标n和m每个是0到300之间的数字，并且该蛋白质额外特征是上述接触角的改变，和此外至少6个用C表示的残基是半胱氨酸。更优选地，所有C表示的氨基酸是半胱氨酸。
优选使用具有通式(III)之蛋白质：
Xn-C1-X5-9-C2-C3-X11-39-C4-X2-23-C5-X5-9-C6-C7-X6-18-C8-Xm (III)
其中X、C及X和C后面之上下标各自系如上文之定义，但下标n及m代表介于0至200间之数字，且该等蛋白质之另一特征系上述接触角之变化。
Xn和Xm残基可以是天然地结合到疏水蛋白的肽序列。然而，一个或两个残基Xn和Xm也可以是天然不结合疏水蛋白的肽序列。这也包Xn和/或Xm残基，其中在疏水蛋白中天然存在的肽序列通过在疏水蛋白中天然不存在的肽序列加长。
当Xn和/或Xm是不天然结合到疏水蛋白的肽序列时，此类序列长为通常至少20个氨基酸，优选至少35个氨基酸，更优选至少50个氨基酸，最优选至少100个氨基酸。此类不天然结合到疏水蛋白的残基在下文中也称作融合配偶体部分。这意在表达根据本发明使用的蛋白质可以由至少一个疏水蛋白部分和在自然中不以该形式一起发生的融合配偶体部分组成。
融合配偶体部分可以选自多种蛋白质。还可能的是多个融合配偶体将结合到一个疏水部分，例如，在疏水蛋白部分上的氨基末端(Xn)和羧基末端(Xm)。然而，还可能例如两个融合配偶体部分将结合到根据本发明使用的蛋白质的一个位置(Xn或Xm)。
尤其适宜之融合配偶体部分系在微生物中(特定言之，在大肠杆菌(E.coli)或枯草芽孢杆菌(Bacillus subtilis)中)天然存在之蛋白质。此等融合配偶体部分之实例系序列yaad(SEQ ID NO：15及16)、yaae(SEQ ID NO：17及18)及硫氧还蛋白。其它高度适宜者系仅包括上述序列之片段或衍生物，其占所述序列之一部分、优选70％至99％且更优选80％至98％，或其中个别氨基酸或核苷酸与所述序列相比已经发生改变者，该等百分比全部基于氨基酸之数目。
本发明所用蛋白质亦可在其多肽序列中受到额外修饰，例如藉由糖基化、乙酰化或者另外藉由化学交联，例如与戊二醛交联。
本发明所用蛋白质之一种性质系当用该等蛋白质涂布表面时表面性质会发生变化。可藉由在用蛋白质涂布表面之前和之后量测水滴之接触角并确定该两次量测间之差来以实验方式确定表面性质之变化。
原则上，本领域技术人员将了解如何实施接触角测量。适于测量接触角之例示性方法的确切实验条件阐述于实验部分中。
迄今已知的疏水蛋白之疏水蛋白部分中的极性及非极性氨基酸位置是受到保护的，由此可获得一特征疏水性曲线图。根据生物物理性质及疏水性之不同可将迄今已知的疏水蛋白划分为2类，I及II(Wessels等人，Ann.Rev.Phytopathol.，1994，32，413-437)。
I型疏水蛋白之组装膜极难溶解(即使在一诸如80℃之高温下于按重量计1％正十二烷基硫酸钠(SDS)水溶液中)且其仅可藉由浓三氟乙酸(TFA)或甲酸重新解离。与之相反，II型疏水蛋白之组装形式较不稳定。II型疏水蛋白仅需藉由按重量计60％乙醇或按重量计1％SDS(各自存于水中，于室温下)即可重新溶解。
氨基酸序列之比较表明：II型疏水蛋白与I型疏水蛋白相比，II型疏水蛋白之半胱氨酸C3与半胱氨酸C4间之区域的长度明显更短。此外，II型疏水蛋白具有较I型疏水蛋白更多的带电荷氨基酸。
用于实施本发明之尤其优选的疏水蛋白系dewA型、rodA型、hypA型、hypB型、sc3型、basf1型、basf2型疏水蛋白，该等疏水蛋白之结构特征示于下文序列表中。其亦可仅为此序列表中之部分或衍生物。亦可将多个(优选为2或3个)具有相同或不同结构之疏水蛋白部分连接在一起并连接至未以天然方式结合至疏水蛋白之对应适宜多肽序列上。
尤其适于实施本发明者亦可为具有示于SEQ ID NO：20、22、24中之多肽序列以及编码SEQ ID NO：20、22、24之核酸序列(特定言之，系SEQID NO：19、21、23序列)的融合蛋白。尤其优选的实施方案进一步包括开始于示于SEQ ID NO.22、22或24中之多肽序列并由至少1个、多达10个、优选5个氨基酸，更优选5％全部氨基酸之替换、插入或缺失而形成且仍具有起始蛋白质之至少50％的生物学性质的蛋白质。本发明所用蛋白质之生物学性质在本文中应理解为意指上述接触角变化至少20°。
本发明所用蛋白质可藉由人们所熟知的肽合成技术(例如，Merrifield固相合成法)以化学方式加以制备。
通过合适的方法可以从天然来源分离天然存在的疏水蛋白。参考例如，
et.al.，Eur.J Cell Bio.63，122-129(1994)或WO 96/41882。
优选通过遗传工程方法可以制备融合蛋白，其中编码融合配偶体的一种核酸序列，特别是DNA序列与编码疏水蛋白部分的一种核酸序列以这样的方式组合使得由于组合的核酸序列的基因表达的结果，在宿主生物中产生所希望的蛋白质。此类制备方法例如公开在我们的先前申请DE102005007480.4中。
用于所提到的制备方法的合适的宿主生物(生产生物)包括原核生物(包括古细菌)或者真核生物，特别是包括嗜盐菌和methanococcia的细菌、真菌、昆虫细胞、植物细胞和哺乳动物细胞，更优选大肠杆菌(Escherichiacoli)、枯草芽孢杆菌(Bacillus subtilis)、巨大芽胞杆菌(Bacillusmegaterium)、米曲霉(Aspergillus oryzea)、构巢曲霉(Aspergillus nidulans)、黑曲霉(Aspergillus niger)、巴斯德毕赤酵母(Pichia pastoris)、假单胞菌(Pseudomonas spec.)、乳杆菌(Lactobacilli)、多形汉逊酵母(Hansenulapolymorpha)、里氏木霉(Trichoderma reesei)、SF9(或相关细胞)，等等。
对于本发明而言，有用的疏水蛋白进一步包括受调控核酸序列基因控制且包含编码本发明所用蛋白质之核酸序列的表达构建体以及包含至少一种这些表达构建体之载体。
所用表达构建体优选包括位于特定编码序列上游5′端之启动子及位于特定编码序列下游3′端之终止子序列以及(若适宜)其它常用调控因子，其各自有效连接至该编码序列。
“有效连接”指启动子、编码序列、终止子和如果合适，其他调节元件的顺序排列，使得每个调节元件可以完成它的如在编码序列的表达中所需的功能。
可有效连接的序列的实例是寻靶序列，和增强子、多聚腺苷酸化信号，等等。其他调节元件包括选择标记、扩增信号、复制起点，等等。合适的调节序列例如描述于Goeddel，Gene Expression Technology：Methods inEnzymology 185，Academic Press，San Diego，CA(1990)。
除了这些调节序列外，这些序列的天然调节可以存在于实际的结构基因的上游，并且如果合适，已经被遗传修饰以便关闭天然调节和增加所述基因的表达。
优选的核酸构建体也有利地包含一个或多个所前述增强子序列，其功能上连接启动子，能够增强核酸序列的表达。还在DNA序列的3’末端，可能插入额外的有利的序列，如其他调节元件或者终止子。
核酸可以以一个或多个拷贝存在于构建体中。如果合适，在构建体中还可包含其他标记，如抗生素抗性或者营养缺陷型互补基因，用于所述构建体的选择。
用于制备的有利的调节序列存在于例如启动子中，如cos、tac、trp、tet、trp-tet、Ipp、lac、Ipp-lac、Iaclq-T7、T5、T3、gal、trc、ara、rhaP(rhaPBAD)SP6、lambda-PR或imlambda-P启动子，其有利地用于革兰氏阴性细菌中。其他有利的调节序列存在于例如革兰氏阳性启动子amy和SP02和酵母或者真菌启动子ADC1、MFalpha、AC、P-60、CYC1、GAPDH、TEF、rp28、ADH中。
还可能使用合成的启动子用于调节。
为了在宿主生物中表达核酸构建体，将核酸构建体有利地插入到载体，如质粒或者噬菌体中，其能够在宿主中最佳地表达基因。除了质粒和噬菌体外，还将载体理解为本领域技术人员已知的所有其他载体，如病毒，如SV40、CMV、杆状病毒和腺病毒、转座子、IS元件、噬粒、粘粒、和线性或环状DNA，以及农杆菌系统。
这些载体可以在宿主生物中自主复制或者在染色体中复制。这些载体构成了本发明的另一形式。合适的质粒为例如，在大肠杆菌中，pLG338、pACYC184、pBR322、pUC18、pUC19、pKC30、pRep4、pHS1、pKK223-3、pDHE19.2、pHS2、pPLc236、pMBL24、pLG200、pUR290、pIN-III”3-B1、tgt11或pBdCI、在链霉菌中，pIJ101、pIJ364、pIJ702或pIJ361，在芽孢杆菌中，pUB110、pC194或pBD214，在棒杆菌中，pSA77或pAJ667、在真菌中，pALS1、pIL2或pBB116，在酵母中，2alpha、pAG-1、YEp6、YEp13或pEMBLYe23或在植物中，pLGV23、pGHIac+、pBIN19、pAK2004或pDH51。所提到的质粒构成了可能的质粒的一小部分。其他质粒是本领域技术人员已知的并且可以例如从书籍Cloning Vectors(Eds.Pouwels P.H.等人Elsevier，Amsterdam-New York-Oxford，1985，ISBN 0444 904018)得到。
有利地，用于表达存在的其他基因的核酸构建体还包含用于增强表达的3’-和/或5’-末端调节序列，其根据所选的宿主生物和基因被选择用于最佳表达。
这些调节序列意在使得能够控制基因表达和蛋白质表达。取决于宿主生物，这可以指例如仅在诱导后基因表达或过表达，或者它可以立即表达和/或过表达。
调节序列或者因子可以优选地积极地影响从而增加所导入的基因的基因表达。从而，通过使用强转录信号，如启动子和/或增强子，可以在转录水平上有利地实现调节元件的增强。此外，还可能通过例如提高mRNA的稳定性增强翻译。
在载体的另一实施方案中，包含核酸构建体或者核酸的载体还可以有利地以线性DNA的形式被导入微生物中并且通过异源或者同源重组整合到宿主生物的基因组中。该线性DNA可以由线性化的载体如质粒组成，或者仅仅由核酸构建体或者核酸组成。
对于异源基因在生物中的最佳表达，有利地根据该生物中使用的特定密码子选择修饰核酸序列。按照其他已知基因在所述生物中的计算机分析，可以容易地确定密码子选择。
通过合适的启动子与合适的编码核苷酸序列和终止子信号或者多聚腺苷酸化信号的融合，可以制备表达盒。为此，使用常规的重组和克隆技术，例如见T.Maniatis，E.F.Fritsch和J.Sambrook，Molecular Cloning：ALaboratory Manual，CoId Spring Harbor Laboratory，Cold SpringHarbor，NY(1989)和T.J.Silhavy，M.L.Berman和L.W.Enquist，Experiments with Gene Fusions，Cold Spring Harbor Laboratory，ColdSpring Harbor，NY(1984)和Ausubel，F.M.等人，Current Protocols inMolecular Biology，Greene Publishing Assoc.and Wiley Interscience(1987)。
为了在合适的宿主生物中表达，有利地将重组核酸构建体或者基因构建体插入到宿主特异性载体中，该载体使得所述基因在宿主中最佳表达。载体是本领域技术人员已知的并且可以例如从“Cloning Vectors”(PouwelsP.H.等人，编著，Elsevier，Amsterdam-New York-Oxford，1985)得到。
借助载体，可能制备重组微生物，其已经例如用至少一种载体转化并且可以用于生产根据本发明使用的蛋白质。有利地，将上述重组构建体导入合适的宿主系统中并表达。优选使用本领域技术人员熟悉的克隆和转染方法，例如，共沉淀、原生质体融合、电穿孔、逆转录病毒转染等等，以便引起所提到的核酸在特定表达系统中表达。合适的系统描述于例如Current Protocols in Molecular Biology，F.Ausubel等人，编著，WileyInterscience，New York 1997或Sambrook等人Molecular Cloning：ALaboratory Manual.第二版，Cold Spring Harbor Laboratory，ColdSpring Harbor Laboratory Press，Cold Spring Harbor，NY，1989。
还可能制备同源重组的微生物。为此，制备包含至少一部分将根据本发明使用的基因或者编码序列的载体，其中如果合适，已经导入至少一个氨基酸缺失、氨基酸添加或者氨基酸替代以便改变，例如功能性破坏该序列(敲除载体)。所导入的序列例如还可以是相关微生物的同源物或者来自哺乳动物、酵母或者昆虫来源。用于同源重组的载体可以备选地这样构造使得对于同源重组的情况，内源基因已经以突变或者改变，但是仍然编码功能蛋白质(例如，可以改变上游调节区使得内源蛋白质的表达改变)。根据本发明使用的基因的改变的部分在同源重组载体中。适于同源重组的载体的构建描述于例如Thomas，K.R.和Capecchi，M.R.(1987)Cell 51：503中。
原则上，对于此类核酸或者此类核酸构建体，所有原核或者真核生物都可以用作重组宿主生物。有利地，使用的宿主生物是微生物，如细菌、真菌或者酵母。优选地，使用革兰氏阳性或者革兰氏阴性细菌，优选来自肠杆菌科(Enterobacteriaceae)、假单胞菌科(Pseudomonadaceae)、根瘤菌科(Rhizobiaceae)、链霉菌科(Streptomycetaceae)或诺卡氏菌科(Nocardiaceae)，更优选埃希氏菌属(Escherichia)、假单胞菌属(Pseudomonas)、链霉菌属(Streptomyces)、诺卡氏菌属(Nocardia)、伯克霍尔德氏菌属(Burkholderia)、沙门氏菌属(Salmonella)、农杆菌属(Agrobacterium)或红球菌属(Rhodococcus)的细菌。
用于上述融合蛋白的制备方法中的生物取决于宿主生物，以本领域技术人员已知的方式生长或培养。微生物通常在液体培养基中在0到100℃，优选10到60℃的温度下在提供氧气下生长，该培养基包含碳源(通常为糖的形式)、氮源(通常为有机氮源的形式，如酵母抽提物)，或者盐，如硫酸铵、微量元素，如铁盐、锰盐和镁盐，以及如果合适，维生素。营养物液体的pH可以保持在固定值，即在培养期间受到调节或者不受调节。可以以分批式、半分批式或者连续发酵式实现培养。营养物可以在发酵开始时导入或者半连续或者连续补充。酶可以通过实施例中描述的方法从生物分离或者作为粗提物用于反应。
可以通过用于重组制备的方法制备本发明的蛋白质、或者其功能性的生物活性片段，在该方法中，培养产生多肽的微生物，如果合适，诱导蛋白质的表达，并将它们从培养物分离。如果希望，还可以在工业规模上以这种方式生产蛋白质。可以通过已知的方法培养和发酵重组微生物。细菌可以例如在TB或者LB培养基中和20到40℃的温度和6到9的pH下繁殖。合适的培养条件特别描述于例如T.Maniatis，E.F.Fritsch和J.Sambrook，Molecular Cloning：A Laboratory Manual，Cold SpringHarbor Laboratory，Cold Spring Harbor，NY(1989)。
如果根据本发明使用的蛋白质不分泌到培养基中，那么将细胞破碎并通过已知的蛋白质分离方法从裂解物得到产物。如果需要，可以通过高频超声波、通过高压、例如，在弗氏压碎器中，通过渗透裂解，通过去污剂的作用，裂解酶或者有机溶剂，通过匀浆器或者通过两种和多种所列方法的组合破碎细胞。
通过已知的层析方法可以纯化本发明的蛋白质，所述方法为诸如分子筛层析(凝胶过滤)，如Q Sepharose层析、离子交换层析和疏水层析，以及使用其他常规的方法，如超滤、结晶、盐析、透析和非变性凝胶电泳。合适的方法描述于例如Cooper，F.G.，Biochemische Arbeitsmethoden[生物化学技术]，Verlag Water de Gruy-ter，Berlin，New York或Scopes，R.，Protein Purification，Springer Verlag，New York，Heidelberg，Berlin。
有利地可藉由使用载体系统或寡核苷酸来分离重组蛋白质，该等寡核苷酸藉由特定核苷酸序列延伸cDNA并藉此编码经改变多肽或用于(例如)简化纯化的融合蛋白。此类适宜修饰之实例系用作锚之“标签”，例如称作六组氨酸锚之修饰或可被抗体识别成抗原之表位(阐述于，例如，Harlow，E.及Lane，D.，1988，Antibodies：A Laboratory Manual.Cold SpringHarbor(N.Y.)Press中)。其它适宜标签系(例如)HA、钙调蛋白-BD、GST、MBD；壳多糖-BD、steptavidin-BD-avi-标记、Flag-标记、T7等。这些锚可用于将蛋白质连接至诸如聚合物基质等固相支持体上，该固相支持体(例如)可填充于层析柱中或可用于微量滴定板上或另一支持体上。对应纯化方案可自市售亲和标记供货商获得。
按照所述制备之蛋白质可直接用作融合蛋白或在切除或去除融合配偶体部分后用作“纯的”疏水蛋白。
当欲去除融合配偶体部分时，建议在融合蛋白中疏水蛋白部分与融合配偶体部分之间引入一潜在的切除位点(蛋白酶之特异性识别位点)。适宜切除位点尤其包括彼等既不会以其它方式出现在疏水蛋白部分亦不会出现在融合配偶体部分中之肽序列，其可藉由生物信息工具容易地测得。尤其适宜者系(例如)甲硫氨酸上之BrCN切除或因子Xa的蛋白酶介导之切除、肠激酶切除、凝血酶、TEV(烟草蚀纹病毒)蛋白酶切除。
当疏水蛋白按照本发明使用时，其实质上可用于涂布表面。优选地，疏水蛋白以水性制剂形式使用。
为实施本发明所进行的疏水蛋白选择基本上不受限制。可使用一种疏水蛋白或者多种不同的疏水蛋白。举例而言，可使用诸如yaad-Xa-dewA-his(SEQ ID NO：19)或yaad-Xa-rodA-his(SEQ ID NO：21)等融合蛋白。
按照本发明，上述疏水蛋白可用于涂布选自织物基质及皮革之纤维基质的表面。
按照本发明，上述疏水蛋白可用于涂布选自织物基质及皮革之纤维基质的表面，而无需藉助于强烷基化化合物(例如氯甲代氧丙环)或交联剂(例如DMDHEU)。
本发明进一步提供一种藉由使用至少一种疏水蛋白涂布选自织物基质及皮革之纤维基质的方法。疏水蛋白、纤维基质、织物基质及皮革以及涂层全部系如上所述。
在本发明之一实施方案中，本发明之方法系藉由使欲涂布纤维基质与至少一种包含至少一疏水蛋白之水性制剂(优选为水溶液)接触来实施。
溶液比可介于(例如)10∶1至1000∶1之间且优选介于70∶1至500∶1之间。
本发明之一实施方案包括藉由浸染方法使欲涂布之纤维基质与至少一种包含至少一疏水蛋白之水性制剂(优选为水溶液)接触。
本发明之另一实施方案包括藉由轧染方法使欲涂布之纤维基质与至少一种包含至少一疏水蛋白之水性制剂(优选为水溶液)接触。
本发明之一实施方案包括使纤维基质尤其是织物基质与疏水蛋白在(例如)一罐中或优选藉由轧染机(pad mangle)接触。
本发明之一实施方案包括在介于0℃至90℃间之温度下且优选介于室温至85℃间之温度下使纤维基质尤其是织物基质与疏水蛋白接触。
本发明之一实施方案包括纤维基质尤其是织物基质，其与疏水蛋白在一罐中或优选藉由一轧染机接触且随后在例如介于20至120℃之温度下干燥。
本发明之一实施方案包括纤维基质尤其是织物基质，其与疏水蛋白在(例如)一罐中或优选藉由一轧染机接触且随后在例如介于20至120℃之温度下干燥一介于5秒至15分钟且优选不超过5分钟之时间段。适宜干燥温度介于(例如)20℃至120℃之间且优选不超过105℃。该温度愈低则干燥时间愈长，且反之亦然。
根据本发明，当藉由一轧染机使纤维基质与疏水蛋白接触时，可选择(例如)介于0.1至10米/分钟且优选介于1至5米/分钟之涂施速度及一介于0.5至4巴之间且优选介于1至3巴之间之辊子接触压力。
本发明之一实施方案包括藉由使用一包括至少一疏水蛋白之水性制剂覆盖(例如藉由喷涂)纤维基质一或多次来使纤维基质尤其是皮革与疏水蛋白接触。
水性制剂可作用于纤维基质上长达(例如)1至24小时且优选为12至17小时。
本发明方法中所用水性制剂优选用水作为溶剂或水与水可混溶性有机溶剂之混合物作为溶剂加以制备。水可混溶性有机溶剂之实例包括水可混溶性一元醇或多元醇，例如甲醇、乙醇、正丙醇、异丙醇、乙二醇、丙二醇或甘油。水可混溶性有机溶剂亦可为醚醇。实例包括(聚)乙二醇或(聚)丙二醇之单烷基醚，例如乙二醇单丁基醚。水溶性有机溶剂之身份及数量本身并不重要且其以本发明所用水性制剂计可介于(例如)1重量％至50重量％之间。
以本发明所用水性制剂计，用于实施本发明方法之水性制剂可进一步包括自0.1至5重量％之无机盐(例如NaCl)。
本发明之一优选实施方案包括不使用诸如氯甲代氧丙环等强烷基化化合物来实施本发明之方法。
本发明之一优选实施方案包括不使用诸如N，N-二羟甲基-4，5-二羟基亚乙基脲(DMDHEU)等交联剂来实施本发明之方法。
制备本发明所用水性制剂且优选为水溶液时，优选可采用经合成、经分离及/或经纯化疏水蛋白水溶液。视其纯度而定，此等亦可包括来自合成之残留辅助剂。当然，亦可在开始时将疏水蛋白作为物质加以分离，例如藉由冷冻干燥，且仅可在第二步骤中配制该等物质。
本发明方法中所用水性制剂中之疏水蛋白之期望浓度可根据欲涂布表面之特征及/或预期用途来确定。但是即使相当低浓度之疏水蛋白亦足以达成期望作用。
在本发明之一实施方案中，本发明之方法利用至少一种包括自1毫克/升至10克/升之至少一种疏水蛋白的水性制剂。
在本发明之一实施方案中，本发明方法中所用水性制剂且尤其是水溶液具有介于3至9之间且优选介于4至8之间之pH。
本发明之一实施方案包括在与疏水蛋白接触之前预处理欲涂布之纤维基质且仅在此后使欲涂布纤维基质与疏水蛋白接触。
预处理之实例系用水、优选使用完全无离子水冲洗若干分钟，更优选冲洗介于5分钟至5小时之间的时间段。
本发明之一实施方案包括藉由使欲按本发明涂布之纤维基质表面与另一包含至少一种活性物质之水性制剂接触来预处理该表面。活性物质可选自有机化学剂(例如阴离子型、阳离子型或非离子型清洁剂)或选自酶(例如蛋白酶或脂肪酶)。
本发明之一实施方案包括按照本发明藉由漂白欲按本发明涂布之纤维基质来实施预处理。当欲涂布纤维基质包括棉花或棉花-合成纤维掺合物时，此实施例为优选的。
本发明所用水性制剂视情况可进一步包括其它组份，例如添加剂及/或辅助剂。此等组份之实例包括酸或碱，例如羧酸或氨；缓冲系统；聚合物；无机颗粒，例如SiO2或硅酸盐；着色剂，例如染料；香料或杀生物剂。添加剂之其它实例陈述于DE-A 101 60 993中，特定言之在第[0074]部分至第[0131]部分。
本发明之方法提供纤维基质之经涂布表面且优选为经涂布织物基质或皮革，其包括一包含至少一种疏水蛋白之防污涂层。
该涂层在经涂布表面上一般包括至少一单分子层疏水蛋白。
根据本发明处理之纤维基质表面(纤维基质系选自织物基质及皮革)不仅具有一经改良之绒状手感及一视觉上均匀的涂层而且具有防尘污作用。
污物通常系指呈固体及/或液体实体形式之硬表面上的任何类别之不期望污染物。污物之实例包括脂肪、油、蛋白质、食物残渣、粉尘或尘土。但污物亦可包括石灰沉积物，例如由于水硬度所形成的水干燥痕迹。其它实例包括个人护理用清洁及护理组合物的残留物或者不溶性石灰皂，该等可由此等清洁及护理组合物结合水硬度形成且可在纤维基质(例如织物基质或皮革)表面上形成沉积物。
防污作用可藉由基本上已知之方法确定，例如藉由用水冲洗来比较未经处理表面与经疏水蛋白处理之表面的污物与该表面之可脱离性。
本发明所用水性制剂可藉由(例如)使一或多种疏水蛋白与水及/或一或多种上述溶剂混合来制备。若需要，可添加其它组份，例如添加剂及/或辅助剂，在此情形中，添加疏水蛋白及水、溶剂(若适宜)及一或多种其它组份(若适宜)之顺序并不关键。
本发明之制剂一般不含强烷基化化合物(例如氯甲代氧丙环)或交联剂(例如DMDHEU)且其可长期储存而不会降解。
本发明进一步提供按照本发明之上述方法涂布之纤维基质(选自织物基质及皮革)。其不仅具有极佳防污性质，而且具有良好洗涤及擦拭坚牢性以及令人愉快之手感。该等经涂布之纤维基质可用于(例如)制造家用织物，例如寝具、帷幔及窗帘、沐浴及卫生织物以及桌布；其进一步可用于制造户外用织物，例如遮阳篷、帐篷、船罩、卡车防水油布、蓬式汽车顶棚且尤其用于制造服装品，例如鞋子、夹克衫、外套、短裤、套衫、长筒袜、腰带以及家用织物，例如寝具、帷幔及窗帘、沐浴及卫生织物以及桌布。根据本发明涂布之皮革尤其适用于制备服装品，例如靴子；以及适于工业用途之空的物品。
下述实施例用于阐释本发明：
部分A：
本发明所用疏水蛋白之制备及测试
实施例1
克隆yaad-His6/yaaE-His6的初步工作
用寡核苷酸Hal570和Hal571(Hal572/Hal573)进行聚合酶链式反应。使用的模板DNA是枯草芽孢杆菌的基因组DNA。所得的PCR片段包含枯草芽孢杆菌yaaD/yaaE基因的编码序列，在每端分别具有NcoI和BgIII限制性切割位点。纯化PCR片段并用限制性内切核酸酶NcoI和BgIII切割。该DNA片段用作插入片段并克隆到来自Qiagen的载体pQE60中，其已经事先用限制性内切核酸酶NcoI和BgIII线性化。所得到的载体pQE60YAAD#2/pQE60YaaE#5可以用于表达由YAAD::HIS6或YAAE::HIS6组成的蛋白质。
Hal570：gcgcgcccatggctcaaacaggtactga
Hal571：gcagatctccagccgcgttcttgcatac
Hal572：ggccatgggattaacaataggtgtactagg
Hal573：gcagatcttacaagtgccttttgcttatattcc
实施例2
克隆yaad疏水蛋白DewA-His6
用寡核苷酸KaM 416和KaM 417进行聚合酶链式反应。使用的模板DNA是构巢曲霉的基因组DNA。所得的PCR片段包含疏水蛋白基因dewA的编码序列和N-末端因子Xa蛋白酶切割位点。纯化PCR片段并用限制性内切核酸酶BamHI切割。该DNA片段用作插入片段并克隆到事先用限制性内切核酸酶BgIII线性化的载体pQE60YAAD#2中。
所形成的载体#508可以用于表达由YAAD::Xa::dewA::HIS6组成的融合蛋白。
KaM416：
GCAGCCCATCAGGGATCCCTCAGCCTTGGTACCAGCGC
KaM417：
CCCGTAGCTAGTGGATCCATTGAAGGCCGCATGAAGTTCTCCGTCTCCGC
实施例3
克隆yaad疏水蛋白RodA-His6
类似地使用寡核苷酸KaM 434和KaM 435将质粒#513克隆到质粒#518中。
KaM434：
GCTAAGCGGATCCATTGAAGGCCGCATGAAGTTCTCCATTGCTGC
KaM435：CCAATGGGGATCCGAGGATGGAGCCAAGGG
实施例4
克隆yaad疏水蛋白BASF1-His6
类似地使用寡核苷酸KaM 417和KaM 418将质粒#507克隆到质粒#508中。使用的模板DNA是人工合成的DNA序列(疏水蛋白BASF1)(见附录)。
KaM417：
CCCGTAGCTAGTGGATCCATTGAAGGCCGCATGAAGTTCTCCGTCTCCGC
KaM418：
CTGCCATTCAGGGGATCCCATATGGAGGAGGGAGACAG
实施例5
克隆yaad疏水蛋白BASF2-His6
类似地使用寡核苷酸KaM 417和KaM 418将质粒#506克隆到质粒#508中。使用的模板DNA是人工合成的DNA序列(疏水蛋白BASF2)(见附录)。
KaM417：
CCCGTAGCTAGTGGATCCATTGAAGGCCGCATGAAGTTCTCCGTCTCCGC
KaM418：
CTGCCATTCAGGGGATCCCATATGGAGGAGGGAGACAG
实施例6
克隆yaad疏水蛋白SC3-His6
类似地使用寡核苷酸KaM 464和KaM 465将质粒#526克隆到质粒#508中。使用的模板DNA是裂褶菌(Schyzophyllum commune)cDNA(见附录)。
KaM464：CGTTAAGGATCCGAGGATGTTGATGGGGGTGC
KaM465：GCTAACAGATCTATGTTCGCCCGTCTCCCCGTCGT
实施例7
重组大肠杆菌菌株yaad疏水蛋白DewA-His6的发酵
在15ml Greiner管中的3ml LB液体培养基中接种表达yaad疏水蛋白DewA-His6的大肠杆菌菌株。在摇床上37℃下以200rpm(转/分钟)培养8小时。两个1升的带挡板的锥形瓶和250ml LB培养基(+100μg/ml氨苄青霉素)在每种情况下接种1ml预培养物并在摇床上以180rpm在37℃下培养9小时。在20升发酵罐中用0.5升预培养物(OD600nm 1∶10，对H2O测量)接种13.5升LB培养基(+100μg/ml氨苄青霉素)。在～3.5的OD600nm下，加入140ml 100mM IPTG。3小时后，冷却发酵罐到10℃并离心除去发酵液。细胞沉淀用于进一步纯化。
实施例8
纯化重组的疏水蛋白融合蛋白(纯化具有C-末端His6标记的疏水蛋白融合蛋白)
将100g细胞沉淀(100-500mg疏水蛋白)用pH 7.5的50mM磷酸钠缓冲液补充到总体积200ml，并重悬浮。将悬浮液用Ultraturrax型T25(Janke和Kunkel；IKA-Labortechnik)处理10分钟并随后在室温下用500单位Benzonase(Merck，Darmstadt；订单号1.01697.0001)温育1小时以降解核酸。细胞破碎前，用玻璃柱体(P1)实现过滤。对于细胞破碎和断裂剩余的基因组DNA，在1500巴下进行两次匀浆器运行(Microfluidizer M-110EH；Microfluidics Corp.)。离心匀浆物(Sorvall RC-5B，GSA-转子，250ml离心杯，60分钟，4℃，12000rpm，23000g)，将上清液置于冰上并将沉淀物重悬浮在100ml磷酸钠缓冲液，pH7.5中。重复离心和重悬浮3次，在第三次重复时磷酸钠缓冲液包含1％SDS。重悬浮后，搅拌混合物1小时并进行最后的离心(Sorvall RC-5B，GSA-转子，250ml离心杯，60分钟，4℃，12000rpm，23000g)。根据SDS-PAGE分析，最后离心后，在上清液中存在疏水蛋白(图1)。实验表明疏水蛋白可能以内含体的形式存在于对应的大肠杆菌细胞中。向用50mM Tris-Cl pH8.0缓冲液平衡的50ml镍-Sepharose HighPerformance 17-5268-02柱(Amersham)应用50ml包含疏水蛋白的上清液。用50mM Tris-Cl pH8.0缓冲液洗涤柱子并随后用包含200mM咪唑的50mM Tris-Cl pH8.0缓冲液洗脱疏水蛋白。为了除去咪唑，对50mM Tris-ClpH8.0缓冲液透析溶液。
图1描绘了所制备的疏水蛋白的纯化：
泳道1：应用于镍-Sepharose柱的溶液(1∶10稀释)
泳道2：穿过液-洗涤步骤洗脱液
泳道3-5：洗脱级分的OD280峰
图1的疏水蛋白具有约53kD的分子量。一些较小的带代表疏水蛋白的降解产物。
实施例9
性能测试；藉由改变水滴在玻璃上之接触角来表征疏水蛋白HP1。
基质：
玻璃(窗户玻璃，Süddeutsche Glas，Mannheim，德国)：
疏水蛋白浓度：100毫克/升
将载玻片在50mM乙酸钠(pH 4)+存于水中之0.1重量％聚氧乙烯(20)去水山梨醇单月桂酸酯中温育15小时(温度80℃)
继而温育，使用蒸馏水洗涤
然后培育：10分钟/80℃/1重量％正-十二烷基硫酸钠水溶液(SDS)
用蒸馏水洗涤
使由此获得的样品经空气干燥(室温)并在室温下测定5微升水滴之接触角(以°计)。
使用Dataphysics Contact Angle System OCA 15+，Software SCA20.2.0.(2002年11月)测定接触角测量值。根据生产商之说明实施该测量。
未经处理玻璃形成30±5°之接触角；含实施例8之功能性疏水蛋白(yaad-dewA-his6)的涂层形成67±5°之接触角。
部分B：
使用疏水蛋白HP1涂布纤维基质表面
该用途测试使用按照实例8所述制备的疏水蛋白(融合蛋白)HP1(yaad-Xa-dewA-his)(SEQ ID NO：19)的溶液。溶液中疏水蛋白HP1之浓度：100毫克/升(0.02重量％)。
B.1本发明织物基质之涂布：
首先使用完全无离子水将白色聚酯纺织物(织物单位重量为226克/米2)冲洗45分钟且随后浸于0.02重量％的HP1水溶液中并在80℃下处理17小时。此后，用完全无离子水将经如此处理之聚酯编织物冲洗1分钟并在室温下干燥以获得本发明处理的基质PES-HP1。该基质PES-HP1具有极为令人满意之手感。
B.2本发明织物基质之涂布
重复B.1，不同之处为在室温下而非80℃下实施该处理。
获得本发明处理基质PES-HP2。该基质PES-HP2具有极为令人满意之手感。
所用污物：
下列物质用作该等测试之污物：
三油精甘油酯
唇膏
废机油
将多个本发明处理基质PES-HP1各自经一种上述污物污染18小时，每平方分米基质使用约0.1克污物。
测试用洗涤组合物之制备及本发明PES-HP1之洗涤
使下列物质混合在一起：
5克 正十二烷基苯磺酸钠
5克 以平均7当量环氧乙烷/摩尔乙氧基化之C13-C15羰基合成醇混合物
5.8克 丙烯酸(70重量％)与马来酸(30重量％)之随机共聚物的40重量％水溶液，经NaOH中和，pH 7.9，Mw70 000克/摩尔。
1.4克 盐析皂
1.2克 Tylose CR 1500p羧甲基纤维素
14克 Na2CO3
30克 沸石A
21克 四水合过硼酸钠
6克 乙二胺四乙酸四钠
3.6克 五水合偏硅酸钠
7克 Na2SO4
以获得测试用洗涤组合物1。
按照本发明处理且随后经污染之PES-HP1样品在来自Atlas，USA之Launder-O-Meter中洗涤，实施3次预洗涤循环及1次主洗涤循环。所用水具有3毫摩尔/升之硬度(Ca∶Mg∶HCO34∶1∶8)，溶液比12.5∶1，剂量为4.5克测试用洗涤组合物1/升，水温40℃。总洗涤时间：30分钟。
彻底清除三油精甘油酯及机油污物，有极少唇膏残留物且其仅在放大镜下可见。
为序列表中的DNA及多肽序列指定序列名称
| dewA DNA及多肽序列 | SEQ ID NO：1 |
| DewA多肽序列 | SEQ ID NO：2 |
| rodA DNA及多肽序列 | SEQ ID NO：3 |
| RodA多肽序列 | SEQ ID NO：4 |
| HypA DNA及多肽序列 | SEQ ID NO：5 |
| HypA多肽序列 | SEQ ID NO：6 |
| HypB DNA及多肽序列 | SEQ ID NO：7 |
| HypB多肽序列 | SEQ ID NO：8 |
| sc3 DNA及多肽序列 | SEQ ID NO：9 |
| sc3多肽序列 | SEQ ID NO：10 |
| basf1 DNA及多肽序列 | SEQ ID NO：11 |
| basf1多肽序列 | SEQ ID NO：12 |
| basf2 DNA及多肽序列 | SEQ ID NO：13 |
| basf2多肽序列 | SEQ ID NO：14 |
| yaad DNA及多肽序列 | SEQ ID NO：15 |
| yaad多肽序列 | SEQ ID NO 16 |
| yaae DNA及多肽序列 | SEQ ID NO：17 |
| yaae多肽序列 | SEQ ID NO：18 |
| yaad-Xa-dewA-his DNA及多肽序列 | SEQ ID NO：19 |
| yaad-Xa-dewA-his多肽序列 | SEQ ID NO：20 |
| yaad-Xa-rodA-his DNA及多肽序列 | SEQ ID NO：21 |
| yaad-Xa-rodA-his多肽序列 | SEQ ID NO：22 |
| yaad-Xa-basf1-his DNA及多肽序列 | SEQ ID NO：23 |
| yaad-Xa-basf1-his多肽序列 | SEQ ID NO：24 |
序列表
<110>巴斯福股份公司
<120>涂布纤维基质表面的方法
<130>AE 20040837
<160>24
<170>PatentIn版本3.1
<210>1
<211>405
<212>DNA
<213>basf-dewA
<220>
<221>CDS
<222>(1)..(405)
<223>
<400>1
atg cgc ttc atc gtc tct ctc ctc gcc ttc act gcc gcg gcc acc gcg 48
Met Arg Phe Ile Val Ser Leu Leu Ala Phe Thr Ala Ala Ala Thr Ala
1 5 10 15
acc gcc ctc ccg gcc tct gcc gca aag aac gcg aag ctg gcc acc tcg 96
Thr Ala Leu Pro Ala Ser Ala Ala Lys Asn Ala Lys Leu Ala Thr Ser
20 25 30
gcg gcc ttc gcc aag cag gct gaa ggc acc acc tgc aat gtc ggc tcg 144
Ala Ala Phe Ala Lys Gln Ala Glu Gly Thr Thr Cys Asn Val Gly Ser
35 40 45
atc gct tgc tgc aac tcc ccc gct gag acc aac aac gac agt ctg ttg 192
Ile Ala Cys Cys Asn Ser Pro Ala Glu Thr Asn Asn Asp Ser Leu Leu
50 55 60
agc ggt ctg ctc ggt gct ggc ctt ctc aac ggg ctc tcg ggc aac act 240
Ser Gly Leu Leu Gly Ala Gly Leu Leu Asn Gly Leu Ser Gly Asn Thr
65 70 75 80
ggc agc gcc tgc gcc aag gcg agc ttg att gac cag ctg ggt ctg ctc 288
Gly Ser Ala Cys Ala Lys Ala Ser Leu Ile Asp Gln Leu Gly Leu Leu
85 90 95
gct ctc gtc gac cac act gag gaa ggc ccc gtc tgc aag aac atc gtc 336
Ala Leu Val Asp His Thr Glu Glu Gly Pro Val Cys Lys Asn Ile Val
100 105 110
gct tgc tgc cct gag gga acc acc aac tgt gtt gcc gtc gac aac gct 384
Ala Cys Cys Pro Glu Gly Thr Thr Asn Cys Val Ala Val Asp Asn Ala
115 120 125
ggc gct ggt acc aag gct gag 405
Gly Ala Gly Thr Lys Ala Glu
130 135
<210>2
<211>135
<212>PRT
<213>basf-dewA
<400>2
Met Arg Phe Ile Val Ser Leu Leu Ala Phe Thr Ala Ala Ala Thr Ala
1 5 10 15
Thr Ala Leu Pro Ala Ser Ala Ala Lys Asn Ala Lys Leu Ala Thr Ser
20 25 30
Ala Ala Phe Ala Lys Gln Ala Glu Gly Thr Thr Cys Asn Val Gly Ser
35 40 45
Ile Ala Cys Cys Asn Ser Pro Ala Glu Thr Asn Asn Asp Ser Leu Leu
50 55 60
Ser Gly Leu Leu Gly Ala Gly Leu Leu Asn Gly Leu Ser Gly Asn Thr
65 70 75 80
Gly Ser Ala Cys Ala Lys Ala Ser Leu Ile Asp Gln Leu Gly Leu Leu
85 90 95
Ala Leu Val Asp His Thr Glu Glu Gly Pro Val Cys Lys Asn Ile Val
100 105 110
Ala Cys Cys Pro Glu Gly Thr Thr Asn Cys Val Ala Val Asp Asn Ala
115 120 125
Gly Ala Gly Thr Lys Ala Glu
130 135
<210>3
<211>471
<212>DNA
<213>basf-rodA
<220>
<221>CDS
<222>(1)..(471)
<223>
<400>3
atg aag ttc tcc att gct gcc gct gtc gtt gct ttc gcc gcc tcc gtc 48
Met Lys Phe Ser Ile Ala Ala Ala Val Val Ala Phe Ala Ala Ser Val
1 5 10 15
gcg gcc ctc cct cct gcc cat gat tcc cag ttc gct ggc aat ggt gtt 96
Ala Ala Leu Pro Pro Ala His Asp Ser Gln Phe Ala Gly Asn Gly Val
20 25 30
ggc aac aag ggc aac agc aac gtc aag ttc cct gtc ccc gaa aac gtg 144
Gly Asn Lys Gly Asn Ser Asn Val Lys Phe Pro Val Pro Glu Asn Val
35 40 45
acc gtc aag cag gcc tcc gac aag tgc ggt gac cag gcc cag ctc tct 192
Thr Val Lys Gln Ala Ser Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser
50 55 60
tgc tgc aac aag gcc acg tac gcc ggt gac acc aca acc gtt gat gag 240
Cys Cys Asn Lys Ala Thr Tyr Ala Gly Asp Thr Thr Thr Val Asp Glu
65 70 75 80
ggt ctt ctg tct ggt gcc ctc agc ggc ctc atc ggc gcc ggg tct ggt 288
Gly Leu Leu Ser Gly Ala Leu Ser Gly Leu Ile Gly Ala Gly Ser Gly
85 90 95
gcc gaa ggt ctt ggt ctc ttc gat cag tgc tcc aag ctt gat gtt gct 336
Ala Glu Gly Leu Gly Leu Phe Asp Gln Cys Ser Lys Leu Asp Val Ala
100 105 110
gtc ctc att ggc atc caa gat ctt gtc aac cag aag tgc aag caa aac 384
Val Leu Ile Gly Ile Gln Asp Leu Val Asn Gln Lys Cys Lys Gln Asn
115 120 125
att gcc tgc tgc cag aac tcc ccc tcc agc gcg gat ggc aac ctt att 432
Ile Ala Cys Cys Gln Asn Ser Pro Ser Ser Ala Asp Gly Asn Leu Ile
130 135 140
ggt gtc ggt ctc cct tgc gtt gcc ctt ggc tcc atc ctc 471
Gly Val Gly Leu Pro Cys Val Ala Leu Gly Ser Ile Leu
145 150 155
<210>4
<211>157
<212>PRT
<213>basf-rodA
<400>4
Met Lys Phe Ser Ile Ala Ala Ala Val Val Ala Phe Ala Ala Ser Val
1 5 10 15
Ala Ala Leu Pro Pro Ala His Asp Ser Gln Phe Ala Gly Asn Gly Val
20 25 30
Gly Asn Lys Gly Asn Ser Asn Val Lys Phe Pro Val Pro Glu Asn Val
35 40 45
Thr Val Lys Gln Ala Ser Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser
50 55 60
Cys Cys Asn Lys Ala Thr Tyr Ala Gly Asp Thr Thr Thr Val Asp Glu
65 70 75 80
Gly Leu Leu Ser Gly Ala Leu Ser Gly Leu Ile Gly Ala Gly Ser Gly
85 90 95
Ala Glu Gly Leu Gly Leu Phe Asp Gln Cys Ser Lys Leu Asp Val Ala
100 105 110
Val Leu Ile Gly Ile Gln Asp Leu Val Asn Gln Lys Cys Lys Gln Asn
115 120 125
Ile Ala Cys Cys Gln Asn Ser Pro Ser Ser Ala Asp Gly Asn Leu Ile
130 135 140
Gly Val Gly Leu Pro Cys Val Ala Leu Gly Ser Ile Leu
145 150 155
<210>5
<211>336
<212>DNA
<213>basf-HypA
<220>
<221>CDS
<222>(1)..(336)
<223>
<400>5
atg atc tct cgc gtc ctt gtc gct gct ctc gtc gct ctc ccc gct ctt 48
Met Ile Ser Arg Val Leu Val Ala Ala Leu Val Ala Leu Pro Ala Leu
1 5 10 15
gtt act gca act cct gct ccc gga aag cct aaa gcc agc agt cag tgc 96
Val Thr Ala Thr Pro Ala Pro Gly Lys Pro Lys Ala Ser Ser Gln Cys
20 25 30
gac gtc ggt gaa atc cat tgc tgt gac act cag cag act ccc gac cac 144
Asp Val Gly Glu Ile His Cys Cys Asp Thr Gln Gln Thr Pro Asp His
35 40 45
acc agc gcc gcc gcg tct ggt ttg ctt ggt gtt ccc atc aac ctt ggt 192
Thr Ser Ala Ala Ala Ser Gly Leu Leu Gly Val Pro Ile Asn Leu Gly
50 55 60
gct ttc ctc ggt ttc gac tgt acc ccc att tcc gtc ctt ggc gtc ggt 240
Ala Phe Leu Gly Phe Asp Cys Thr Pro Ile Ser Val Leu Gly Val Gly
65 70 75 80
ggc aac aac tgt gct gct cag cct gtc tgc tgc aca gga aat caa ttc 288
Gly Asn Asn Cys Ala Ala Gln Pro Val Cys Cys Thr Gly Asn Gln Phe
85 90 95
acc gca ttg att aac gct ctt gac tgc tct cct gtc aat gtc aac ctc 336
Thr Ala Leu Ile Asn Ala Leu Asp Cys Ser Pro Val Asn Val Asn Leu
100 105 110
<210>6
<211>112
<212>PRT
<213>basf-HypA
<400>6
Met Ile Ser Arg Val Leu Val Ala Ala Leu Val Ala Leu Pro Ala Leu
1 5 10 15
Val Thr Ala Thr Pro Ala Pro Gly Lys Pro Lys Ala Ser Ser Gln Cys
20 25 30
Asp Val Gly Glu Ile His Cys Cys Asp Thr Gln Gln Thr Pro Asp His
35 40 45
Thr Ser Ala Ala Ala Ser Gly Leu Leu Gly Val Pro Ile Asn Leu Gly
50 55 60
Ala Phe Leu Gly Phe Asp Cys Thr Pro Ile Ser Val Leu Gly Val Gly
65 70 75 80
Gly Asn Asn Cys Ala Ala Gln Pro Val Cys Cys Thr Gly Asn Gln Phe
85 90 95
Thr Ala Leu Ile Asn Ala Leu Asp Cys Ser Pro Val Asn Val Asn Leu
100 105 110
<210>7
<211>357
<212>DNA
<213>basf-HypB
<220>
<221>CDS
<222>(1)..(357)
<223>
<400>7
atg gtc agc acg ttc atc act gtc gca aag acc ctt ctc gtc gcg ctc 48
Met Val Ser Thr Phe Ile Thr Val Ala Lys Thr Leu Leu Val Ala Leu
1 5 10 15
ctc ttc gtc aat atc aat atc gtc gtt ggt act gca act acc ggc aag 96
Leu Phe Val Asn Ile Asn Ile Val Val Gly Thr Ala Thr Thr Gly Lys
20 25 30
cat tgt agc acc ggt cct atc gag tgc tgc aag cag gtc atg gat tct 144
His Cys Ser Thr Gly Pro Ile Glu Cys Cys Lys Gln Val Met Asp Ser
35 40 45
aag agc cct cag gct acg gag ctt ctt acg aag aat ggc ctt ggc ctg 192
Lys Ser Pro Gln Ala Thr Glu Leu Leu Thr Lys Asn Gly Leu Gly Leu
50 55 60
ggt gtc ctt gct ggc gtg aag ggt ctt gtt ggc gcg aat tgc agc cct 240
Gly Val Leu Ala Gly Val Lys Gly Leu Val Gly Ala Asn Cys Ser Pro
65 70 75 80
atc acg gca att ggt att ggc tcc ggc agc caa tgc tct ggc cag acc 288
Ile Thr Ala Ile Gly Ile Gly Ser Gly Ser Gln Cys Ser Gly Gln Thr
85 90 95
gtt tgc tgc cag aat aat aat ttc aac ggt gtt gtc gct att ggt tgc 336
Val Cys Cys Gln Asn Asn Asn Phe Asn Gly Val Val Ala Ile Gly Cys
100 105 110
act ccc att aat gcc aat gtg 357
Thr Pro Ile Asn Ala Asn Val
115
<210>8
<211>119
<212>PRT
<213>basf-HypB
<400>8
Met Val Ser Thr Phe Ile Thr Val Ala Lys Thr Leu Leu Val Ala Leu
1 5 10 15
Leu Phe Val Asn Ile Asn Ile Val Val Gly Thr Ala Thr Thr Gly Lys
20 25 30
His Cys Ser Thr Gly Pro Ile Glu Cys Cys Lys Gln Val Met Asp Ser
35 40 45
Lys Ser Pro Gln Ala Thr Glu Leu Leu Thr Lys Asn Gly Leu Gly Leu
50 55 60
Gly Val Leu Ala Gly Val Lys Gly Leu Val Gly Ala Asn Cys Ser Pro
65 70 75 80
Ile Thr Ala Ile Gly Ile Gly Ser Gly Ser Gln Cys Ser Gly Gln Thr
85 90 95
Val Cys Cys Gln Asn Asn Asn Phe Asn Gly Val Val Ala Ile Gly Cys
100 105 110
Thr Pro Ile Asn Ala Asn Val
115
<210>9
<211>408
<212>DNA
<213>basf-sc3
<220>
<221>CDS
<222>(1)..(408)
<223>
<400>9
atg ttc gcc cgt ctc ccc gtc gtg ttc ctc tac gcc ttc gtc gcg ttc 48
Met Phe Ala Arg Leu Pro Val Val Phe Leu Tyr Ala Phe Val Ala Phe
1 5 10 15
ggc gcc ctc gtc gct gcc ctc cca ggt ggc cac ccg ggc acg acc acg 96
Gly Ala Leu Val Ala Ala Leu Pro Gly Gly His Pro Gly Thr Thr Thr
20 25 30
ccg ccg gtt acg acg acg gtg acg gtg acc acg ccg ccc tcg acg acg 144
Pro Pro Val Thr Thr Thr Val Thr Val Thr Thr Pro Pro Ser Thr Thr
35 40 45
acc atc gcc gcc ggt ggc acg tgt act acg ggg tcg ctc tct tgc tgc 192
Thr Ile Ala Ala Gly Gly Thr Cys Thr Thr Gly Ser Leu Ser Cys Cys
50 55 60
aac cag gtt caa tcg gcg agc agc agc cct gtt acc gcc ctc ctc ggc 240
Asn Gln Val Gln Ser Ala Ser Ser Ser Pro Val Thr Ala Leu Leu Gly
65 70 75 80
ctg ctc ggc att gtc ctc agc gac ctc aac gtt ctc gtt ggc atc agc 288
Leu Leu Gly Ile Val Leu Ser Asp Leu Asn Val Leu Val Gly Ile Ser
85 90 95
tgc tct ccc ctc act gtc atc ggt gtc gga ggc agc ggc tgt tcg gcg 336
Cys Ser Pro Leu Thr Val Ile Gly Val Gly Gly Ser Gly Cys Ser Ala
100 105 110
cag acc gtc tgc tgc gaa aac acc caa ttc aac ggg ctg atc aac atc 384
Gln Thr Val Cys Cys Glu Asn Thr Gln Phe Asn Gly Leu Ile Asn Ile
115 120 125
ggt tgc acc ccc atc aac atc ctc 408
Gly Cys Thr Pro Ile Asn Ile Leu
130 135
<210>10
<211>136
<212>PRT
<213>basf-sc3
<400>10
Met Phe Ala Arg Leu Pro Val Val Phe Leu Tyr Ala Phe Val Ala Phe
1 5 10 15
Gly Ala Leu Val Ala Ala Leu Pro Gly Gly His Pro Gly Thr Thr Thr
20 25 30
Pro Pro Val Thr Thr Thr Val Thr Val Thr Thr Pro Pro Ser Thr Thr
35 40 45
Thr Ile Ala Ala Gly Gly Thr Cys Thr Thr Gly Ser Leu Ser Cys Cys
50 55 60
Asn Gln Val Gln Ser Ala Ser Ser Ser Pro Val Thr Ala Leu Leu Gly
65 70 75 80
Leu Leu Gly Ile Val Leu Ser Asp Leu Asn Val Leu Val Gly Ile Ser
85 90 95
Cys Ser Pro Leu Thr Val Ile Gly Val Gly Gly Ser Gly Cys Ser Ala
100 105 110
Gln Thr Val Cys Cys Glu Asn Thr Gln Phe Asn Gly Leu Ile Asn Ile
115 120 125
Gly Cys Thr Pro Ile Asn Ile Leu
130 135
<210>11
<211>483
<212>DNA
<213>basf-BASF1
<220>
<221>CDS
<222>(1)..(483)
<223>
<400>11
atg aag ttc tcc gtc tcc gcc gcc gtc ctc gcc ttc gcc gcc tcc gtc 48
Met Lys Phe Ser Val Ser Ala Ala Val Leu Ala Phe Ala Ala Ser Val
1 5 10 15
gcc gcc ctc cct cag cac gac tcc gcc gcc ggc aac ggc aac ggc gtc 96
Ala Ala Leu Pro Gln His Asp Ser Ala Ala Gly Asn Gly Asn Gly Val
20 25 30
ggc aac aag ttc cct gtc cct gac gac gtc acc gtc aag cag gcc acc 144
Gly Asn Lys Phe Pro Val Pro Asp Asp Val Thr Val Lys Gln Ala Thr
35 40 45
gac aag tgc ggc gac cag gcc cag ctc tcc tgc tgc aac aag gcc acc 192
Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys Ala Thr
50 55 60
tac gcc ggc gac gtc ctc acc gac atc gac gag ggc atc ctc gcc ggc 240
Tyr Ala Gly Asp Val Leu Thr Asp Ile Asp Glu Gly Ile Leu Ala Gly
65 70 75 80
ctc ctc aag aac ctc atc ggc ggc ggc tcc ggc tcc gag ggc ctc ggc 288
Leu Leu Lys Asn Leu Ile Gly Gly Gly Ser Gly Ser Glu Gly Leu Gly
85 90 95
ctc ttc gac cag tgc gtc aag ctc gac ctc cag atc tcc gtc atc ggc 336
Leu Phe Asp Gln Cys Val Lys Leu Asp Leu Gln Ile Ser Val Ile Gly
100 105 110
atc cct atc cag gac ctc ctc aac cag gtc aac aag cag tgc aag cag 384
Ile Pro Ile Gln Asp Leu Leu Asn Gln Val Asn Lys Gln Cys Lys Gln
115 120 125
aac atc gcc tgc tgc cag aac tcc cct tcc gac gcc acc ggc tcc ctc 432
Asn Ile Ala Cys Cys Gln Asn Ser Pro Ser Asp Ala Thr Gly Ser Leu
130 135 140
gtc aac ctc ggc ctc ggc aac cct tgc atc cct gtc tcc ctc ctc cat 480
Val Asn Leu Gly Leu Gly Asn Pro Cys Ile Pro Val Ser Leu Leu His
145 150 155 160
atg 483
Met
<210>12
<211>161
<212>PRT
<213>basf-BASF1
<400>12
Met Lys Phe Ser Val Ser Ala Ala Val Leu Ala Phe Ala Ala Ser Val
1 5 10 15
Ala Ala Leu Pro Gln His Asp Ser Ala Ala Gly Asn Gly Asn Gly Val
20 25 30
Gly Asn Lys Phe Pro Val Pro Asp Asp Val Thr Val Lys Gln Ala Thr
35 40 45
Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys Ala Thr
50 55 60
Tyr Ala Gly Asp Val Leu Thr Asp Ile Asp Glu Gly Ile Leu Ala Gly
65 70 75 80
Leu Leu Lys Asn Leu Ile Gly Gly Gly Ser Gly Ser Glu Gly Leu Gly
85 90 95
Leu Phe Asp Gln Cys Val Lys Leu Asp Leu Gln Ile Ser Val Ile Gly
100 105 110
Ile Pro Ile Gln Asp Leu Leu Asn Gln Val Asn Lys Gln Cys Lys Gln
115 120 125
Asn Ile Ala Cys Cys Gln Asn Ser Pro Ser Asp Ala Thr Gly Ser Leu
130 135 140
Val Asn Leu Gly Leu Gly Asn Pro Cys Ile Pro Val Ser Leu Leu His
145 150 155 160
Met
<210>13
<211>465
<212>DNA
<213>basf-BASF2
<220>
<221>CDS
<222>(1)..(465)
<223>
<400>13
atg aag ttc tcc gtc tcc gcc gcc gtc ctc gcc ttc gcc gcc tcc gtc 48
Met Lys Phe Ser Val Ser Ala Ala Val Leu Ala Phe Ala Ala Ser Val
1 5 10 15
gcc gcc ctc cct cag cac gac tcc gcc gcc ggc aac ggc aac ggc gtc 96
Ala Ala Leu Pro Gln His Asp Ser Ala Ala Gly Asn Gly Asn Gly Val
20 25 30
ggc aac aag ttc cct gtc cct gac gac gtc acc gtc aag cag gcc acc 144
Gly Asn Lys Phe Pro Val Pro Asp Asp Val Thr Val Lys Gln Ala Thr
35 40 45
gac aag tgc ggc gac cag gcc cag ctc tcc tgc tgc aac aag gcc acc 192
Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys Ala Thr
50 55 60
tac gcc ggc gac gtc acc gac atc gac gag ggc atc ctc gcc ggc ctc 240
Tyr Ala Gly Asp Val Thr Asp Ile Asp Glu Gly Ile Leu Ala Gly Leu
65 70 75 80
ctc aag aac ctc atc ggc ggc ggc tcc ggc tcc gag ggc ctc ggc ctc 288
Leu Lys Asn Leu Ile Gly Gly Gly Ser Gly Ser Glu Gly Leu Gly Leu
85 90 95
ttc gac cag tgc gtc aag ctc gac ctc cag atc tcc gtc atc ggc atc 336
Phe Asp Gln Cys Val Lys Leu Asp Leu Gln Ile Ser Val Ile Gly Ile
100 105 110
cct atc cag gac ctc ctc aac cag cag tgc aag cag aac atc gcc tgc 384
Pro Ile Gln Asp Leu Leu Asn Gln Gln Cys Lys Gln Asn Ile Ala Cys
115 120 125
tgc cag aac tcc cct tcc gac gcc acc ggc tcc ctc gtc aac ctc ggc 432
Cys Gln Asn Ser Pro Ser Asp Ala Thr Gly Ser Leu Val Asn Leu Gly
130 135 140
aac cct tgc atc cct gtc tcc ctc ctc cat atg 465
Asn Pro Cys Ile Pro Val Ser Leu Leu His Met
145 150 155
<210>14
<211>155
<212>PRT
<213>basf-BASF2
<400>14
Met Lys Phe Ser Val Ser Ala Ala Val Leu Ala Phe Ala Ala Ser Val
1 5 10 15
Ala Ala Leu Pro Gln His Asp Ser Ala Ala Gly Asn Gly Asn Gly Val
20 25 30
Gly Asn Lys Phe Pro Val Pro Asp Asp Val Thr Val Lys Gln Ala Thr
35 40 45
Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys Ala Thr
50 55 60
Tyr ALa Gly Asp Val Thr Asp Ile Asp Glu Gly Ile Leu Ala Gly Leu
65 70 75 80
Leu Lys Asn Leu Ile Gly Gly Gly Ser Gly Ser Glu Gly Leu Gly Leu
85 90 95
Phe Asp Gln Cys Val Lys Leu Asp Leu Gln Ile Ser Val Ile Gly Ile
100 105 110
Pro Ile Gln Asp Leu Leu Asn Gln Gln Cys Lys Gln Asn Ile Ala Cys
115 120 125
Cys Gln Asn Ser Pro Ser Asp Ala Thr Gly Ser Leu Val Asn Leu Gly
130 135 140
Asn Pro Cys Ile Pro Val Ser Leu Leu His Met
145 150 155
<210>15
<211>882
<212>DNA
<213>basf-yaad
<220>
<221>CDS
<222>(1)..(882)
<223>
<400>15
atg gct caa aca ggt act gaa cgt gta aaa cgc gga atg gca gaa atg 48
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
caa aaa ggc ggc gtc atc atg gac gtc atc aat gcg gaa caa gcg aaa 96
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
atc gct gaa gaa gct gga gct gtc gct gta atg gcg cta gaa cgt gtg 144
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
cca gca gat att cgc gcg gct gga gga gtt gcc cgt atg gct gac cct 192
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
aca atc gtg gaa gaa gta atg aat gca gta tct atc ccg gta atg gca 240
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
aaa gcg cgt atc gga cat att gtt gaa gcg cgt gtg ctt gaa gct atg 288
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
ggt gtt gac tat att gat gaa agt gaa gtt ctg acg ccg gct gac gaa 336
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
gaa ttt cat tta aat aaa aat gaa tac aca gtt cct ttt gtc tgt ggc 384
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
tgc cgt gat ctt ggt gaa gca aca cgc cgt att gcg gaa ggt gct tct 432
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
atg ctt cgc aca aaa ggt gag cct gga aca ggt aat att gtt gag gct 480
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
gtt cgc cat atg cgt aaa gtt aac gct caa gtg cgc aaa gta gtt gcg 528
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
atg agt gag gat gag cta atg aca gaa gcg aaa aac cta ggt gct cct 576
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
tac gag ctt ctt ctt caa att aaa aaa gac ggc aag ctt cct gtc gtt 624
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
aac ttt gcc gct ggc ggc gta gca act cca gct gat gct gct ctc atg 672
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
atg cag ctt ggt gct gac gga gta ttt gtt ggt tct ggt att ttt aaa 720
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
tca gac aac cct gct aaa ttt gcg aaa gca att gtg gaa gca aca act 768
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
cac ttt act gat tac aaa tta atc gct gag ttg tca aaa gag ctt ggt 816
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
act gca atg aaa ggg att gaa atc tca aac tta ctt cca gaa cag cgt 864
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
atg caa gaa cgc ggc tgg 882
Met Gln Glu Arg Gly Trp
290
<210>16
<211>294
<212>PRT
<213>basf-yaad
<400>16
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
Met Gln Glu Arg Gly Trp
290
<210>17
<211>591
<212>DNA
<213>basf-yaae
<220>
<221>CDS
<222>(1)..(591)
<223>
<400>17
atg gga tta aca ata ggt gta cta gga ctt caa gga gca gtt aga gag 48
Met Gly Leu Thr Ile Gly Val Leu Gly Leu Gln Gly Ala Val Arg Glu
1 5 10 15
cac atc cat gcg att gaa gca tgc ggc gcg gct ggt ctt gtc gta aaa 96
His Ile His Ala Ile Glu Ala Cys Gly Ala Ala Gly Leu Val Val Lys
20 25 30
cgt ccg gag cag ctg aac gaa gtt gac ggg ttg att ttg ccg ggc ggt 144
Arg Pro Glu Gln Leu Asn Glu Val Asp Gly Leu Ile Leu Pro Gly Gly
35 40 45
gag agc acg acg atg cgc cgt ttg atc gat acg tat caa ttc atg gag 192
Glu Ser Thr Thr Met Arg Arg Leu Ile Asp Thr Tyr Gln Phe Met Glu
50 55 60
ccg ctt cgt gaa ttc gct gct cag ggc aaa ccg atg ttt gga aca tgt 240
Pro Leu Arg Glu Phe Ala Ala Gln Gly Lys Pro Met Phe Gly Thr Cys
657 0 75 80
gcc gga tta att ata tta gca aaa gaa att gcc ggt tca gat aat cct 288
Ala Gly Leu Ile Ile Leu Ala Lys Glu Ile Ala Gly Ser Asp Asn Pro
85 90 95
cat tta ggt ctt ctg aat gtg gtt gta gaa cgt aat tca ttt ggc cgg 336
His Leu Gly Leu Leu Asn Val Val Val Glu Arg Asn Ser Phe Gly Arg
100 105 110
cag gtt gac agc ttt gaa gct gat tta aca att aaa ggc ttg gac gag 384
Gln Val Asp Ser Phe Glu Ala Asp Leu Thr Ile Lys Gly Leu Asp Glu
115 120 125
cct ttt act ggg gta ttc atc cgt gct ccg cat att tta gaa gct ggt 432
Pro Phe Thr Gly Val Phe Ile Arg Ala Pro His Ile Leu Glu Ala Gly
130 135 140
gaa aat gtt gaa gtt cta tcg gag cat aat ggt cgt att gta gcc gcg 480
Glu Asn Val Glu Val Leu Ser Glu His Asn Gly Arg Ile Val Ala Ala
145 150 155 160
aaa cag ggg caa ttc ctt ggc tgc tca ttc cat ccg gag ctg aca gaa 528
Lys Gln Gly Gln Phe Leu Gly Cys Ser Phe His Pro Glu Leu Thr Glu
165 170 175
gat cac cga gtg acg cag ctg ttt gtt gaa atg gtt gag gaa tat aag 576
Asp His Arg Val Thr Gln Leu Phe Val Glu Met Val Glu Glu Tyr Lys
180 185 190
caa aag gca ctt gta 591
Gln Lys Ala Leu Val
195
<210>18
<211>197
<212>PRT
<213>basf-yaae
<400>18
Met Gly Leu Thr Ile Gly Val Leu Gly Leu Gln Gly Ala Val Arg Glu
1 5 10 15
His Ile His Ala Ile Glu Ala Cys Gly Ala Ala Gly Leu Val Val Lys
20 25 30
Arg Pro Glu Gln Leu Asn Glu Val Asp Gly Leu Ile Leu Pro Gly Gly
35 40 45
Glu Ser Thr Thr Met Arg Arg Leu Ile Asp Thr Tyr Gln Phe Met Glu
50 55 60
Pro Leu Arg Glu Phe Ala Ala Gln Gly Lys Pro Met Phe Gly Thr Cys
65 70 75 80
Ala Gly Leu Ile Ile Leu Ala Lys Glu Ile Ala Gly Ser Asp Asn Pro
85 90 95
His Leu Gly Leu Leu Asn Val Val Val Glu Arg Asn Ser Phe Gly Arg
100 105 110
Gln Val Asp Ser Phe Glu Ala Asp Leu Thr Ile Lys Gly Leu Asp Glu
115 120 125
Pro Phe Thr Gly Val Phe Ile Arg Ala Pro His Ile Leu Glu Ala Gly
130 135 140
Glu Asn Val Glu Val Leu Ser Glu His Asn Gly Arg Ile Val Ala Ala
145 150 155 160
Lys Gln Gly Gln Phe Leu Gly Cys Ser Phe His Pro Glu Leu Thr Glu
165 170 175
Asp His Arg Val Thr Gln Leu Phe Val Glu Met Val Glu Glu Tyr Lys
180 185 190
Gln Lys Ala Leu Val
195
<210>19
<211>1329
<212>DNA
<213>basf-yaad-Xa-dewA-his
<220>
<221>CDS
<222>(1)..(1329)
<223>
<400>19
atg gct caa aca ggt act gaa cgt gta aaa cgc gga atg gca gaa atg 48
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
caa aaa ggc ggc gtc atc atg gac gtc atc aat gcg gaa caa gcg aaa 96
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
atc gct gaa gaa gct gga gct gtc gct gta atg gcg cta gaa cgt gtg 144
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
cca gca gat att cgc gcg gct gga gga gtt gcc cgt atg gct gac cct 192
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
aca atc gtg gaa gaa gta atg aat gca gta tct atc ccg gta atg gca 240
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
aaa gcg cgt atc gga cat att gtt gaa gcg cgt gtg ctt gaa gct atg 288
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
ggt gtt gac tat att gat gaa agt gaa gtt ctg acg ccg gct gac gaa 336
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
gaa ttt cat tta aat aaa aat gaa tac aca gtt cct ttt gtc tgt ggc 384
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
tgc cgt gat ctt ggt gaa gca aca cgc cgt att gcg gaa ggt gct tct 432
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
atg ctt cgc aca aaa ggt gag cct gga aca ggt aat att gtt gag gct 480
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
gtt cgc cat atg cgt aaa gtt aac gct caa gtg cgc aaa gta gtt gcg 528
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
atg agt gag gat gag cta atg aca gaa gcg aaa aac cta ggt gct cct 576
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
tac gag ctt ctt ctt caa att aaa aaa gac ggc aag ctt cct gtc gtt 624
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
aac ttt gcc gct ggc ggc gta gca act cca gct gat gct gct ctc atg 672
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
atg cag ctt ggt gct gac gga gta ttt gtt ggt tct ggt att ttt aaa 720
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
tca gac aac cct gct aaa ttt gcg aaa gca att gtg gaa gca aca act 768
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
cac ttt act gat tac aaa tta atc gct gag ttg tca aaa gag ctt ggt 816
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
act gca atg aaa ggg att gaa atc tca aac tta ctt cca gaa cag cgt 864
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
atg caa gaa cgc ggc tgg aga tcc att gaa ggc cgc atg cgc ttc atc 912
Met Gln Glu Arg Gly Trp Arg Ser Ile Glu Gly Arg Met Arg Phe Ile
290 295 300
gtc tct ctc ctc gcc ttc act gcc gcg gcc acc gcg acc gcc ctc ccg 960
Val Ser Leu Leu Ala Phe Thr Ala Ala Ala Thr Ala Thr Ala Leu Pro
305 310 315 320
gcc tct gcc gca aag aac gcg aag ctg gcc acc tcg gcg gcc ttc gcc 1008
Ala Ser Ala Ala Lys Asn Ala Lys Leu Ala Thr Ser Ala Ala Phe Ala
325 330 335
aag cag gct gaa ggc acc acc tgc aat gtc ggc tcg atc gct tgc tgc 1056
Lys Gln Ala Glu Gly Thr Thr Cys Asn Val Gly Ser Ile Ala Cys Cys
340 345 350
aac tcc ccc gct gag acc aac aac gac agt ctg ttg agc ggt ctg ctc 1104
Asn Ser Pro Ala Glu Thr Asn Asn Asp Ser Leu Leu Ser Gly Leu Leu
355 360 365
ggt gct ggc ctt ctc aac ggg ctc tcg ggc aac act ggc agc gcc tgc 1152
Gly Ala Gly Leu Leu Asn Gly Leu Ser Gly Asn Thr Gly Ser Ala Cys
370 375 380
gcc aag gcg agc ttg att gac cag ctg ggt ctg ctc gct ctc gtc gac 1200
Ala Lys Ala Ser Leu Ile Asp Gln Leu Gly Leu Leu Ala Leu Val Asp
385 390 395 400
cac act gag gaa ggc ccc gtc tgc aag aac atc gtc gct tgc tgc cct 1248
His Thr Glu Glu Gly Pro Val Cys Lys Asn Ile Val Ala Cys Cys Pro
405 410 415
gag gga acc acc aac tgt gtt gcc gtc gac aac gct ggc gct ggt acc 1296
Glu Gly Thr Thr Asn Cys Val Ala Val Asp Asn Ala Gly Ala Gly Thr
420 425 430
aag gct gag gga tct cat cac cat cac cat cac 1329
Lys Ala Glu Gly Ser His His His His His His
435 440
<210>20
<211>443
<212>PRT
<213>basf-yaad-Xa-dewA-his
<400>20
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
Met Gln Glu Arg Gly Trp Arg Ser Ile Glu Gly Arg Met Arg Phe Ile
290 295 300
Val Ser Leu Leu Ala Phe Thr Ala Ala Ala Thr Ala Thr Ala Leu Pro
305 310 315 320
Ala Ser Ala Ala Lys Asn Ala Lys Leu Ala Thr Ser Ala Ala Phe Ala
325 330 335
Lys Gln Ala Glu Gly Thr Thr Cys Asn Val Gly Ser Ile Ala Cys Cys
340 345 350
Asn Ser Pro Ala Glu Thr Asn Asn Asp Ser Leu Leu Ser Gly Leu Leu
355 360 365
Gly Ala Gly Leu Leu Asn Gly Leu Ser Gly Asn Thr Gly Ser Ala Cys
370 375 380
Ala Lys Ala Ser Leu Ile Asp Gln Leu Gly Leu Leu Ala Leu Val Asp
385 390 395 400
His Thr Glu Glu Gly Pro Val Cys Lys Asn Ile Val Ala Cys Cys Pro
405 410 415
Glu Gly Thr Thr Asn Cys Val Ala Val Asp Asn Ala Gly Ala Gly Thr
420 425 430
Lys Ala Glu Gly Ser His His His His His His
435 440
<210>21
<211>1395
<212>DNA
<213>basf-yaad-Xa-rodA-his
<220>
<221>CDS
<222>(1)..(1395)
<223>
<400>21
atg gct caa aca ggt act gaa cgt gta aaa cgc gga atg gca gaa atg 48
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
caa aaa ggc ggc gtc atc atg gac gtc atc aat gcg gaa caa gcg aaa 96
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
atc gct gaa gaa gct gga gct gtc gct gta atg gcg cta gaa cgt gtg 144
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
cca gca gat att cgc gcg gct gga gga gtt gcc cgt atg gct gac cct 192
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
aca atc gtg gaa gaa gta atg aat gca gta tct atc ccg gta atg gca 240
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
aaa gcg cgt atc gga cat att gtt gaa gcg cgt gtg ctt gaa gct atg 288
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
ggt gtt gac tat att gat gaa agt gaa gtt ctg acg ccg gct gac gaa 336
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
gaa ttt cat tta aat aaa aat gaa tac aca gtt cct ttt gtc tgt ggc 384
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
tgc cgt gat ctt ggt gaa gca aca cgc cgt att gcg gaa ggt gct tct 432
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
atg ctt cgc aca aaa ggt gag cct gga aca ggt aat att gtt gag gct 480
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
gtt cgc cat atg cgt aaa gtt aac gct caa gtg cgc aaa gta gtt gcg 528
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
atg agt gag gat gag cta atg aca gaa gcg aaa aac cta ggt gct cct 576
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
tac gag ctt ctt ctt caa att aaa aaa gac ggc aag ctt cct gtc gtt 624
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
aac ttt gcc gct ggc ggc gta gca act cca gct gat gct gct ctc atg 672
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
atg cag ctt ggt gct gac gga gta ttt gtt ggt tct ggt att ttt aaa 720
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser GlyIle Phe Lys
225 230 235 240
tca gac aac cct gct aaa ttt gcg aaa gca att gtg gaa gca aca act 768
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
cac ttt act gat tac aaa tta atc gct gag ttg tca aaa gag ctt ggt 816
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
act gca atg aaa ggg att gaa atc tca aac tta ctt cca gaa cag cgt 864
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
atg caa gaa cgc ggc tgg aga tct att gaa ggc cgc atg aag ttc tcc 912
Met Gln Glu Arg Gly Trp Arg Ser Ile Glu Gly Arg Met Lys Phe Ser
290 295 300
att gct gcc gct gtc gtt gct ttc gcc gcc tcc gtc gcg gcc ctc cct 960
Ile Ala Ala Ala Val Val Ala Phe Ala Ala Ser Val Ala Ala Leu Pro
305 310 315 320
cct gcc cat gat tcc cag ttc gct ggc aat ggt gtt ggc aac aag ggc 1008
Pro Ala His Asp Ser Gln Phe Ala Gly Asn Gly Val Gly Asn Lys Gly
325 330 335
aac agc aac gtc aag ttc cct gtc ccc gaa aac gtg acc gtc aag cag 1056
Asn Ser Asn Val Lys Phe Pro Val Pro Glu Asn Val Thr Val Lys Gln
340 345 350
gcc tcc gac aag tgc ggt gac cag gcc cag ctc tct tgc tgc aac aag 1104
Ala Ser Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys
355 360 365
gcc acg tac gcc ggt gac acc aca acc gtt gat gag ggt ctt ctg tct 1152
Ala Thr Tyr Ala Gly Asp Thr Thr Thr Val Asp Glu Gly Leu Leu Ser
370 375 380
ggt gcc ctc agc ggc ctc atc ggc gcc ggg tct ggt gcc gaa ggt ctt 1200
Gly Ala Leu Ser Gly Leu Ile Gly Ala Gly Ser Gly Ala Glu Gly Leu
385 390 395 400
ggt ctc ttc gat cag tgc tcc aag ctt gat gtt gct gtc ctc att ggc 1248
Gly Leu Phe Asp Gln Cys Ser Lys Leu Asp Val Ala Val Leu Ile Gly
405 410 415
atc caa gat ctt gtc aac cag aag tgc aag caa aac att gcc tgc tgc 1296
Ile Gln Asp Leu Val Asn Gln Lys Cys Lys Gln Asn Ile Ala Cys Cys
420 425 430
cag aac tcc ccc tcc agc gcg gat ggc aac ctt att ggt gtc ggt ctc 1344
Gln Asn Ser Pro Ser Ser Ala Asp Gly Asn Leu Ile Gly Val Gly Leu
435 440 445
cct tgc gtt gcc ctt ggc tcc atc ctc gga tct cat cac cat cac cat 1392
Pro Cys Val Ala Leu Gly Ser Ile Leu Gly Ser His His His His His
450 455 460
cac 1395
His
465
<210>22
<211>465
<212>PRT
<213>basf-yaad-Xa-rodA-his
<400>22
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
Met Gln Glu Arg Gly Trp Arg Ser Ile Glu Gly Arg Met Lys Phe Ser
290 295 300
Ile Ala Ala Ala Val Val Ala Phe Ala Ala Ser Val Ala Ala Leu Pro
305 310 315 320
Pro Ala His Asp Ser Gln Phe Ala Gly Asn Gly Val Gly Asn Lys Gly
325 330 335
Asn Ser Asn Val Lys Phe Pro Val Pro Glu Asn Val Thr Val Lys Gln
340 345 350
Ala Ser Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys
355 360 365
Ala Thr Tyr Ala Gly Asp Thr Thr Thr Val Asp Glu Gly Leu Leu Ser
370 375 380
Gly Ala Leu Ser Gly Leu Ile Gly Ala Gly Ser Gly Ala Glu Gly Leu
385 390 395 400
Gly Leu Phe Asp Gln Cys Ser Lys Leu Asp Val Ala Val Leu Ile Gly
405 410 415
Ile Gln Asp Leu Val Asn Gln Lys Cys Lys Gln Asn Ile Ala Cys Cys
420 425 430
Gln Asn Ser Pro Ser Ser Ala Asp Gly Asn Leu Ile Gly Val Gly Leu
435 440 445
Pro Cys Val Ala Leu Gly Ser Ile Leu Gly Ser His His His His His
450 455 460
His
465
<210>23
<211>1407
<212>DNA
<213>basf-yaad-Xa-BASF1-his
<220>
<221>CDS
<222>(1)..(1407)
<223>
<400>23
atg gct caa aca ggt act gaa cgt gta aaa cgc gga atg gca gaa atg 48
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
caa aaa ggc ggc gtc atc atg gac gtc atc aat gcg gaa caa gcg aaa 96
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
atc gct gaa gaa gct gga gct gtc gct gta atg gcg cta gaa cgt gtg 144
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
cca gca gat att cgc gcg gct gga gga gtt gcc cgt atg gct gac cct 192
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
aca atc gtg gaa gaa gta atg aat gca gta tct atc ccg gta atg gca 240
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
aaa gcg cgt atc gga cat att gtt gaa gcg cgt gtg ctt gaa gct atg 288
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
ggt gtt gac tat att gat gaa agt gaa gtt ctg acg ccg gct gac gaa 336
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
gaa ttt cat tta aat aaa aat gaa tac aca gtt cct ttt gtc tgt ggc 384
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
tgc cgt gat ctt ggt gaa gca aca cgc cgt att gcg gaa ggt gct tct 432
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
atg ctt cgc aca aaa ggt gag cct gga aca ggt aat att gtt gag gct 480
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
gtt cgc cat atg cgt aaa gtt aac gct caa gtg cgc aaa gta gtt gcg 528
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
atg agt gag gat gag cta atg aca gaa gcg aaa aac cta ggt gct cct 576
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
tac gag ctt ctt ctt caa att aaa aaa gac ggc aag ctt cct gtc gtt 624
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
aac ttt gcc gct ggc ggc gta gca act cca gct gat gct gct ctc atg 672
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
atg cag ctt ggt gct gac gga gta ttt gtt ggt tct ggt att ttt aaa 720
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
tca gac aac cct gct aaa ttt gcg aaa gca att gtg gaa gca aca act 768
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
cac ttt act gat tac aaa tta atc gct gag ttg tca aaa gag ctt ggt 816
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
act gca atg aaa ggg att gaa atc tca aac tta ctt cca gaa cag cgt 864
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
atg caa gaa cgc ggc tgg aga tct att gaa ggc cgc atg aag ttc tcc 912
Met Gln Glu Arg Gly Trp Arg Ser Ile Glu Gly Arg Met Lys Phe Ser
290 295 300
gtc tcc gcc gcc gtc ctc gcc ttc gcc gcc tcc gtc gcc gcc ctc cct 960
Val Ser Ala Ala Val Leu Ala Phe Ala Ala Ser Val Ala Ala Leu Pro
305 310 315 320
cag cac gac tcc gcc gcc ggc aac ggc aac ggc gtc ggc aac aag ttc 1008
Gln His Asp Ser Ala Ala Gly Asn Gly Asn Gly Val Gly Asn Lys Phe
325 330 335
cct gtc cct gac gac gtc acc gtc aag cag gcc acc gac aag tgc ggc 1056
Pro Val Pro Asp Asp Val Thr Val Lys Gln Ala Thr Asp Lys Cys Gly
340 345 350
gac cag gcc cag ctc tcc tgc tgc aac aag gcc acc tac gcc ggc gac 1104
Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys Ala Thr Tyr Ala Gly Asp
355 360 365
gtc ctc acc gac atc gac gag ggc atc ctc gcc ggc ctc ctc aag aac 1152
Val Leu Thr Asp Ile Asp Glu Gly Ile Leu Ala Gly Leu Leu Lys Asn
370 375 380
ctc atc ggc ggc ggc tcc ggc tcc gag ggc ctc ggc ctc ttc gac cag 1200
Leu Ile Gly Gly Gly Ser Gly Ser Glu Gly Leu Gly Leu Phe Asp Gln
385 390 395 400
tgc gtc aag ctc gac ctc cag atc tcc gtc atc ggc atc cct atc cag 1248
Cys Val Lys Leu Asp Leu Gln Ile Ser Val Ile Gly Ile Pro Ile Gln
405 410 415
gac ctc ctc aac cag gtc aac aag cag tgc aag cag aac atc gcc tgc 1296
Asp Leu Leu Asn Gln Val Asn Lys Gln Cys Lys Gln Asn Ile Ala Cys
420 425 430
tgc cag aac tcc cct tcc gac gcc acc ggc tcc ctc gtc aac ctc ggc 1344
Cys Gln Asn Ser Pro Ser Asp Ala Thr Gly Ser Leu Val Asn Leu Gly
435 440 445
ctc ggc aac cct tgc atc cct gtc tcc ctc ctc cat atg gga tct cat 1392
Leu Gly Asn Pro Cys Ile Pro Val Ser Leu Leu His Met Gly Ser His
450 455 460
cac cat cac cat cac 1407
His His His His His
465
<210>24
<211>469
<212>PRT
<213>basf-yaad-Xa-BASF1-his
<400>24
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
Met Gln Glu Arg Gly Trp Arg Ser Ile Glu Gly Arg Met Lys Phe Ser
290 295 300
Val Ser Ala Ala Val Leu Ala Phe Ala Ala Ser Val Ala Ala Leu Pro
305 310 315 320
Gln His Asp Ser Ala Ala Gly Asn Gly Asn Gly Val Gly Asn Lys Phe
325 330 335
Pro Val Pro Asp Asp Val Thr Val Lys Gln Ala Thr Asp Lys Cys Gly
340 345 350
Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys Ala Thr Tyr Ala Gly Asp
355 360 365
Val Leu Thr Asp Ile Asp Glu Gly Ile Leu Ala Gly Leu Leu Lys Asn
370 375 380
Leu Ile Gly Gly Gly Ser Gly Ser Glu Gly Leu Gly Leu Phe Asp Gln
385 390 395 400
Cys Val Lys Leu Asp Leu Gln Ile Ser Val Ile Gly Ile Pro Ile Gln
405 410 415
Asp Leu Leu Asn Gln Val Asn Lys Gln Cys Lys Gln Asn Ile Ala Cys
420 425 430
Cys Gln Asn Ser Pro Ser Asp Ala Thr Gly Ser Leu Val Asn Leu Gly
435 440 445
Leu Gly Asn Pro Cys Ile Pro Val Ser Leu Leu His Met Gly Ser His
450 455 460
His His His His His
465
Claims (9)
1.通过使用至少一种疏水蛋白来涂布选自织物基质及皮革的纤维基质的方法。
2.权利要求1的方法，其是通过将纤维材料与至少一种包含至少一种疏水蛋白的水性制剂接触来完成的。
3.权利要求1或2的方法，其在轧染机中实施。
4.权利要求1到3任一项的方法，其利用至少一种包含1毫克/升至10克/升范围内的至少一种疏水蛋白的水性制剂。
5.权利要求1到4任一项的方法，其中纤维基质经预处理且然后与疏水蛋白接触。
6.权利要求1到5任一项的方法，其中将纤维基质与疏水蛋白接触后，在20℃至120℃范围内的温度下实施干燥。
7.根据权利要求1到6至少一项涂布的纤维基质。
8.使用至少一种根据权利要求7的纤维基质生产的服装、家用织物、工业用织物、衣服用或工业用皮革品。
9.疏水蛋白用于涂布选自织物基质及皮革的纤维基质表面的用途。
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE200510026143 DE102005026143A1 (de) | 2005-06-06 | 2005-06-06 | Verfahren zur Beschichtung von Oberflächen von faserigen Substraten |
| DE102005026143.4 | 2005-06-06 | ||
| DE102005030786.8 | 2005-06-29 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN101180431A true CN101180431A (zh) | 2008-05-14 |
Family
ID=37402021
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CNA2006800172586A Pending CN101180431A (zh) | 2005-06-06 | 2006-05-31 | 纤维基质表面的涂布 |
Country Status (3)
| Country | Link |
|---|---|
| CN (1) | CN101180431A (zh) |
| DE (1) | DE102005026143A1 (zh) |
| ZA (1) | ZA200800094B (zh) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106567247A (zh) * | 2016-10-25 | 2017-04-19 | 东莞市联洲知识产权运营管理有限公司 | 一种抗蛋白质污染的再生纤维素织物的制备方法 |
-
2005
- 2005-06-06 DE DE200510026143 patent/DE102005026143A1/de not_active Withdrawn
-
2006
- 2006-05-31 CN CNA2006800172586A patent/CN101180431A/zh active Pending
-
2008
- 2008-01-04 ZA ZA200800094A patent/ZA200800094B/xx unknown
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106567247A (zh) * | 2016-10-25 | 2017-04-19 | 东莞市联洲知识产权运营管理有限公司 | 一种抗蛋白质污染的再生纤维素织物的制备方法 |
Also Published As
| Publication number | Publication date |
|---|---|
| ZA200800094B (en) | 2009-10-28 |
| DE102005026143A1 (de) | 2006-12-07 |
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Open date: 20080514 |