JPH0335000A - Production of crosslinked collagen or crosslinked gelatin - Google Patents
Production of crosslinked collagen or crosslinked gelatinInfo
- Publication number
- JPH0335000A JPH0335000A JP16915389A JP16915389A JPH0335000A JP H0335000 A JPH0335000 A JP H0335000A JP 16915389 A JP16915389 A JP 16915389A JP 16915389 A JP16915389 A JP 16915389A JP H0335000 A JPH0335000 A JP H0335000A
- Authority
- JP
- Japan
- Prior art keywords
- collagen
- gelatin
- carbon atoms
- formula
- crosslinked
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 108010035532 Collagen Proteins 0.000 title claims abstract description 55
- 102000008186 Collagen Human genes 0.000 title claims abstract description 55
- 229920001436 collagen Polymers 0.000 title claims abstract description 55
- 108010010803 Gelatin Proteins 0.000 title claims abstract description 42
- 229920000159 gelatin Polymers 0.000 title claims abstract description 42
- 239000008273 gelatin Substances 0.000 title claims abstract description 42
- 235000019322 gelatine Nutrition 0.000 title claims abstract description 42
- 235000011852 gelatine desserts Nutrition 0.000 title claims abstract description 42
- 238000004519 manufacturing process Methods 0.000 title claims description 11
- 239000003431 cross linking reagent Substances 0.000 claims abstract description 33
- 238000004132 cross linking Methods 0.000 claims abstract description 21
- 238000006243 chemical reaction Methods 0.000 claims abstract description 16
- 125000003545 alkoxy group Chemical group 0.000 claims abstract description 10
- 125000003282 alkyl amino group Chemical group 0.000 claims abstract description 10
- 125000000217 alkyl group Chemical group 0.000 claims abstract description 10
- 125000005843 halogen group Chemical group 0.000 claims abstract description 8
- 150000003918 triazines Chemical class 0.000 claims abstract description 5
- 239000000243 solution Substances 0.000 claims description 28
- 125000004432 carbon atom Chemical group C* 0.000 claims description 20
- 125000004435 hydrogen atom Chemical group [H]* 0.000 claims description 7
- 239000000126 substance Substances 0.000 claims description 7
- 239000000725 suspension Substances 0.000 claims description 4
- JYEUMXHLPRZUAT-UHFFFAOYSA-N 1,2,3-triazine Chemical compound C1=CN=NN=C1 JYEUMXHLPRZUAT-UHFFFAOYSA-N 0.000 claims description 3
- 230000002378 acidificating effect Effects 0.000 claims description 2
- 230000007935 neutral effect Effects 0.000 claims description 2
- HMSBXLTWCMFPDZ-UHFFFAOYSA-N 2,4-dichloro-6-ethoxy-1,3,5-triazine Chemical compound CCOC1=NC(Cl)=NC(Cl)=N1 HMSBXLTWCMFPDZ-UHFFFAOYSA-N 0.000 claims 1
- JKAPWXKZLYJQJJ-UHFFFAOYSA-N 2,4-dichloro-6-methoxy-1,3,5-triazine Chemical group COC1=NC(Cl)=NC(Cl)=N1 JKAPWXKZLYJQJJ-UHFFFAOYSA-N 0.000 claims 1
- 125000004429 atom Chemical group 0.000 claims 1
- 239000003637 basic solution Substances 0.000 claims 1
- 150000001875 compounds Chemical class 0.000 abstract description 4
- 150000003230 pyrimidines Chemical class 0.000 abstract description 3
- 150000004867 thiadiazoles Chemical class 0.000 abstract description 3
- 150000000095 trithianes Chemical class 0.000 abstract description 3
- FYADHXFMURLYQI-UHFFFAOYSA-N 1,2,4-triazine Chemical class C1=CN=NC=N1 FYADHXFMURLYQI-UHFFFAOYSA-N 0.000 abstract description 2
- 229910052736 halogen Inorganic materials 0.000 abstract 3
- 150000002367 halogens Chemical class 0.000 abstract 1
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 18
- 238000000034 method Methods 0.000 description 14
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 10
- -1 aldehyde compounds Chemical class 0.000 description 9
- 239000012670 alkaline solution Substances 0.000 description 9
- 108010045569 atelocollagen Proteins 0.000 description 6
- 239000002253 acid Substances 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical class [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 239000003960 organic solvent Substances 0.000 description 4
- FIDRAVVQGKNYQK-UHFFFAOYSA-N 1,2,3,4-tetrahydrotriazine Chemical compound C1NNNC=C1 FIDRAVVQGKNYQK-UHFFFAOYSA-N 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 3
- ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 3
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 3
- JUJWROOIHBZHMG-UHFFFAOYSA-N Pyridine Chemical compound C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 3
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 description 3
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 3
- 238000011282 treatment Methods 0.000 description 3
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 239000004593 Epoxy Chemical class 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 2
- WYURNTSHIVDZCO-UHFFFAOYSA-N Tetrahydrofuran Chemical compound C1CCOC1 WYURNTSHIVDZCO-UHFFFAOYSA-N 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 125000004106 butoxy group Chemical group [*]OC([H])([H])C([H])([H])C(C([H])([H])[H])([H])[H] 0.000 description 2
- 150000001845 chromium compounds Chemical class 0.000 description 2
- 150000007529 inorganic bases Chemical class 0.000 description 2
- 239000012948 isocyanate Substances 0.000 description 2
- 150000007530 organic bases Chemical class 0.000 description 2
- 229940083082 pyrimidine derivative acting on arteriolar smooth muscle Drugs 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- DQXNTSXKIUZJJS-UHFFFAOYSA-N 2,4-dichloro-5-methylpyrimidine Chemical class CC1=CN=C(Cl)N=C1Cl DQXNTSXKIUZJJS-UHFFFAOYSA-N 0.000 description 1
- ZTNVNAIEXWYGML-UHFFFAOYSA-N 2-butoxy-4,6-dichloro-1,3,5-triazine Chemical compound CCCCOC1=NC(Cl)=NC(Cl)=N1 ZTNVNAIEXWYGML-UHFFFAOYSA-N 0.000 description 1
- ZSLUVFAKFWKJRC-IGMARMGPSA-N 232Th Chemical compound [232Th] ZSLUVFAKFWKJRC-IGMARMGPSA-N 0.000 description 1
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical group [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 1
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-M Bicarbonate Chemical compound OC([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-M 0.000 description 1
- WKBOTKDWSSQWDR-UHFFFAOYSA-N Bromine atom Chemical group [Br] WKBOTKDWSSQWDR-UHFFFAOYSA-N 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- FXHOOIRPVKKKFG-UHFFFAOYSA-N N,N-Dimethylacetamide Chemical compound CN(C)C(C)=O FXHOOIRPVKKKFG-UHFFFAOYSA-N 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 229910052776 Thorium Inorganic materials 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- HOPRXXXSABQWAV-UHFFFAOYSA-N anhydrous collidine Natural products CC1=CC=NC(C)=C1C HOPRXXXSABQWAV-UHFFFAOYSA-N 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 229910052801 chlorine Inorganic materials 0.000 description 1
- 125000001309 chloro group Chemical group Cl* 0.000 description 1
- UTBIMNXEDGNJFE-UHFFFAOYSA-N collidine Natural products CC1=CC=C(C)C(C)=N1 UTBIMNXEDGNJFE-UHFFFAOYSA-N 0.000 description 1
- 239000004020 conductor Substances 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 125000002147 dimethylamino group Chemical group [H]C([H])([H])N(*)C([H])([H])[H] 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 125000001301 ethoxy group Chemical group [H]C([H])([H])C([H])([H])O* 0.000 description 1
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 1
- 125000000031 ethylamino group Chemical group [H]C([H])([H])C([H])([H])N([H])[*] 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 239000003292 glue Substances 0.000 description 1
- 125000000623 heterocyclic group Chemical group 0.000 description 1
- 229910052740 iodine Inorganic materials 0.000 description 1
- 125000003253 isopropoxy group Chemical group [H]C([H])([H])C([H])(O*)C([H])([H])[H] 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 239000010985 leather Substances 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 125000000956 methoxy group Chemical group [H]C([H])([H])O* 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 239000012046 mixed solvent Substances 0.000 description 1
- BDERNNFJNOPAEC-UHFFFAOYSA-N propan-1-ol Chemical compound CCCO BDERNNFJNOPAEC-UHFFFAOYSA-N 0.000 description 1
- 125000001436 propyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- UMJSCPRVCHMLSP-UHFFFAOYSA-N pyridine Natural products COC1=CC=CN=C1 UMJSCPRVCHMLSP-UHFFFAOYSA-N 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- UIIMBOGNXHQVGW-UHFFFAOYSA-M sodium bicarbonate Substances [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- GFYHSKONPJXCDE-UHFFFAOYSA-N sym-collidine Natural products CC1=CN=C(C)C(C)=C1 GFYHSKONPJXCDE-UHFFFAOYSA-N 0.000 description 1
- 125000004213 tert-butoxy group Chemical group [H]C([H])([H])C(O*)(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- YLQBMQCUIZJEEH-UHFFFAOYSA-N tetrahydrofuran Natural products C=1C=COC=1 YLQBMQCUIZJEEH-UHFFFAOYSA-N 0.000 description 1
- VLLMWSRANPNYQX-UHFFFAOYSA-N thiadiazole Chemical compound C1=CSN=N1.C1=CSN=N1 VLLMWSRANPNYQX-UHFFFAOYSA-N 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
Landscapes
- Artificial Filaments (AREA)
- Peptides Or Proteins (AREA)
Abstract
Description
【発明の詳細な説明】
〔産業上の利用分野〕
本発明は架橋コラ−ケンまたは架橋セラチンの製造方法
に関し、更に詳しくは無色でかつ優れた物理的強度を有
する架橋コラーゲンまたは架橋ゼラチンの製造方法に関
する。[Detailed Description of the Invention] [Industrial Application Field] The present invention relates to a method for producing cross-linked collagen or cross-linked seratin, and more specifically, a method for producing cross-linked collagen or gelatin that is colorless and has excellent physical strength. Regarding.
コラーゲンは動物の結合組織を構成するタンパク質であ
り、古代から皮革、膠等として利用されている。近年は
コラーゲンが生体由来であることから、食品、化粧品や
医療への応用が行われている。特に皮膚などに含まれる
不溶性のコラーゲンを可溶化する技４ホｉが確立される
に伴い、さらにその応用が広がっている。可溶化したコ
ラーゲンを応用するには、組織を利用する時と同様に物
理的強度の向上、あるいは耐吸収性の向上を図るため、
化学薬品、γ線などの手段により架橋処理される。Collagen is a protein that constitutes the connective tissue of animals, and has been used in leather, glue, etc. since ancient times. In recent years, since collagen is derived from living organisms, it has been applied to foods, cosmetics, and medicine. In particular, with the establishment of techniques for solubilizing insoluble collagen contained in the skin, its applications are further expanding. When applying solubilized collagen, it is necessary to improve its physical strength or absorption resistance in the same way as when using tissue.
Cross-linking treatment is performed by means such as chemicals and gamma rays.
従来この架橋処理に使用される化学薬品としては、クロ
ム化合物、アルデヒド化合物、イソシアナート化合物、
エポキシ化合物などが知られている。Chemicals conventionally used for this crosslinking treatment include chromium compounds, aldehyde compounds, isocyanate compounds,
Epoxy compounds are known.
しかし、これらの架橋処理に使用される化学薬品には次
のような種々の問題点があった。すなわち、クロム化合
物の場合は架橋物が濃く着色してしまう。またアルデヒ
ド化合物の場合は代表的なグルタルアルデヒドでさえも
架橋物が黄色に着色し、無色の架橋物を必要とする際に
問題となる。However, the chemicals used in these crosslinking treatments have the following various problems. That is, in the case of a chromium compound, the crosslinked product becomes darkly colored. In the case of aldehyde compounds, even the typical glutaraldehyde produces a yellow colored crosslinked product, which poses a problem when a colorless crosslinked product is required.
またイソシアナート化合物の場合は水との反応性が高い
ため架橋反応が煩雑となる欠点があった。Further, in the case of isocyanate compounds, there is a drawback that crosslinking reactions are complicated because of their high reactivity with water.
さらにエポキシ化合物の場合ば親水性が強いため架橋物
が著しく膨潤してしまう欠点があった。Furthermore, in the case of epoxy compounds, there is a drawback that the crosslinked product swells significantly due to its strong hydrophilicity.
本発明の目的は上記した問題点の解消にあり、無色でか
つ優れた物理的強度を有する架橋コラーゲンまたは架橋
ゼラチンの製造方法を提供することである。An object of the present invention is to solve the above-mentioned problems, and to provide a method for producing crosslinked collagen or gelatin that is colorless and has excellent physical strength.
本発明者等は上記した目的を達成すべく鋭意研究を重ね
た結果、トリアジン誘導体などの活性へテロ環ポリハラ
イドを架橋剤として用いたところ、無色でかつ優れた物
理的強度を有する架橋コラーゲンまたは架橋ゼラチンが
得られることを見出し、本発明を完成するに到った。As a result of intensive research to achieve the above-mentioned object, the present inventors have found that by using active heterocyclic polyhalides such as triazine derivatives as crosslinking agents, crosslinked collagen or crosslinked collagen, which is colorless and has excellent physical strength, has been found. It was discovered that gelatin could be obtained, and the present invention was completed.
すなわち、本発明の架橋コラ−ケンまたは架橋ゼラチン
の製造方法は、
ＲＩ Ｒ２
３
（式中、Ｒ１乃至Ｒ３は同一であっても異なってもよく
、少なくとも２つがハロゲン原子を表し、残りが水素原
子、炭素数１〜３のアルキル基、炭素数１〜４のアルコ
キシ基または炭素数１〜３のアルキルアミノ基を表ず）
で示されるトリアジン誘導（式中、Ｒ１乃至Ｒ３は前記
と同義である）で示されるトリチアン誘導体、
−であっても異なってもよ＜、Ｒ４およびＲ６の少なく
とも１つがハロゲン原子を表し、残りが水素原子、炭素
数１〜３のアルキル基、炭素数１〜４のアルコキシ基ま
たは炭素数１〜３のアルキルアミノ基を表し、Ｒ５は水
素原子、炭素数１〜３のアル・）・ル基、炭素数１〜４
のアルコキシ基、炭素数１〜３のアルキルアミノ基を表
す）で示されるピリミジン誘導体および
（式中、Ｘは前記と同義である）で示されるチアジアゾ
ール誘導体よりなる群から選択される少なくとも１種の
架橋剤とコラ−ケンまたは＃橋セラチンとを塩基性条件
下に架橋反応させることを特徴とするものである。That is, the method for producing crosslinked kolaken or crosslinked gelatin of the present invention is based on RI R2 3 (wherein R1 to R3 may be the same or different, at least two represent halogen atoms, and the remaining are hydrogen atoms) , does not represent an alkyl group having 1 to 3 carbon atoms, an alkoxy group having 1 to 4 carbon atoms, or an alkylamino group having 1 to 3 carbon atoms)
A trithiane derivative represented by a triazine derivative (wherein R1 to R3 are as defined above), which may be - or different, at least one of R4 and R6 represents a halogen atom, and the remaining Represents a hydrogen atom, an alkyl group having 1 to 3 carbon atoms, an alkoxy group having 1 to 4 carbon atoms, or an alkylamino group having 1 to 3 carbon atoms, and R5 is a hydrogen atom or an alkyl group having 1 to 3 carbon atoms. , carbon number 1-4
At least one type selected from the group consisting of pyrimidine derivatives represented by (representing an alkoxy group or an alkylamino group having 1 to 3 carbon atoms) and thiadiazole derivatives represented by (wherein, X is as defined above) It is characterized by carrying out a crosslinking reaction between a crosslinking agent and Kolaken or #bridged Seratin under basic conditions.
本発明の方法に使用されるコラーゲンまたはゼラチンは
一般にコラ−ケンまたはセラチンとして知られているも
のであれば特別に制限されず、例えば、通常のコラ−ケ
ンまたはゼラチン、アテロコラーゲン、コラーゲンを含
む生体組織などが挙げられる。Collagen or gelatin used in the method of the present invention is not particularly limited as long as it is generally known as collagen or seratin, and examples include ordinary collagen or gelatin, atelocollagen, and biological tissue containing collagen. Examples include.
本発明の方法に使用される架橋剤はコラーゲンまたはゼ
ラチンとの架橋反応性に冨むものであって、前記一般式
で示されるトリアジン誘導体、トリチアン誘導体、ピリ
ミジン誘導体およびチアジアゾールＭＡ ８体よりなる
’ＢＹから選択された少なくとも１種のものである。The crosslinking agent used in the method of the present invention is one that is rich in crosslinking reactivity with collagen or gelatin, and is composed of 'BY' consisting of triazine derivatives, trithiane derivatives, pyrimidine derivatives, and thiadiazole MA 8 bodies represented by the above general formula. At least one selected type.
ここで、式中、ハロゲン原子とはフ、素原子、塩素原子
、臭素原子、ヨウ素原子を意味し、炭素数１〜３のアル
キル基とはメチル基、エチル基、プロピル基、イソプロ
ピル基を意味し、炭素数１〜４のアルコキシ基とはメト
キシ基、エトキシ基、プ丁コボキシ基、イソプロポキシ
基、ブトキシ基、５ｅＣ−ブトキシ基、ｔｅｒｔ−ブＩ
・キシ基を意味し、炭素数１〜３のアルキルアミノ基と
はメチルアくノ基、ジメチルアミノ基、エチルアミノ基
、メチルエチルアミノ基を意味する。Here, in the formula, the halogen atom means a hydrogen atom, a chlorine atom, a bromine atom, or an iodine atom, and the alkyl group having 1 to 3 carbon atoms means a methyl group, an ethyl group, a propyl group, or an isopropyl group. However, the alkoxy group having 1 to 4 carbon atoms refers to methoxy group, ethoxy group, butoxy group, isopropoxy group, butoxy group, 5eC-butoxy group, tert-butoxy group,
- Means an xy group, and an alkylamino group having 1 to 3 carbon atoms means a methylacuno group, a dimethylamino group, an ethylamino group, and a methylethylamino group.
この架橋剤の具体例としては、２，４．６−クリクロロ
−１，３，５−トリアジン、２．４−シクｌ］じ；−６
−メドキシーＬ３，５− １−リアジン、２，４−ジク
ロロ−６−ニドキシ−１，３，５−トリアジン、２，４
−ジクロロ−６−ブトキシ−１，３，５−トリアジン、
２．４−ジクロロ−６−メチル１、．３．５− ）リ
アジンなどのトリアジン誘導体；２゜４．６− トリク
ロロ−Ｌ３，５− トリアチン、２，４−ジクロロ−
６−メドキシーＬ３，５− １−リチアン、２４−ジク
ロロ−６−ニトキシー１，３，５− ）リチアン、２
，４−ジクロ０−６−プトキシーＬ３，５−ｈリチアン
、２，４−ジクロロ−６−メチル−１３５−トリチアン
などのトリアジン導体； ２，４．６− トリク［１０
−１，３− ピリミジン、２４−ジクｏｐ−１，３−ピ
リミジン、２，４−シクｌ’ｌ ｌ−１５７トキシー１
．３−ビリ宅ジン、２．４−ジクロロ−５エトキシ−１
３−ピリくジン、２，４−ジクロロ−５−フトキシー１
．３− ピリミジン、２，４−ジクロロ−５−メチル−
１，３−ピリミジンなどのピリミジン誘１体；２゜５−
ジクロロ−Ｌ３，４−チアジアゾール、２，５−シブロ
ミドー１３．４−チアジアゾールなどのチアジアゾール
誘導体が挙げられる。これらの架橋剤の中でも、コラー
ゲンまたはゼラチンとの架橋反応性に冨みまた入手の容
易性を考慮すると、２，４．６− トリク１コロ−１，
３，５−トリアジン、２．４＝シクロ０−６−メドキシ
ーＬ３５−１−リアジン、２，４−ジクロロ−６−ニト
キシーＬ３，５− トリアジンの使用が好ましい。Specific examples of this crosslinking agent include 2,4,6-chloro-1,3,5-triazine, 2,4-cyclo]di;-6
-Medoxy L3,5- 1-Riazine, 2,4-dichloro-6-nidoxy-1,3,5-triazine, 2,4
-dichloro-6-butoxy-1,3,5-triazine,
2.4-dichloro-6-methyl 1,. 3.5-) Triazine derivatives such as riazine; 2゜4.6-trichloro-L3,5-triatine, 2,4-dichloro-
6-medoxy L3,5- 1-lithian, 24-dichloro-6-nitoxyl, 3,5-) lithian, 2
,4-dichloro0-6-ptoxyL3,5-hrithiane, triazine conductors such as 2,4-dichloro-6-methyl-135-trithiane; 2,4.6-tric[10
-1,3-pyrimidine, 24-di-op-1,3-pyrimidine, 2,4-cyc-l'l-157 toxic 1
．． 3-Biriyakuzine, 2,4-dichloro-5ethoxy-1
3-pyridine, 2,4-dichloro-5-phthoxyl 1
．． 3-pyrimidine, 2,4-dichloro-5-methyl-
Pyrimidine derivatives such as 1,3-pyrimidine; 2゜5-
Examples include thiadiazole derivatives such as dichloro-L3,4-thiadiazole and 2,5-sibromido-13,4-thiadiazole. Among these crosslinking agents, 2,4.6-Triku1 Coro-1,
Preference is given to using 3,5-triazine, 2,4=cyclo0-6-medoxy L35-1-riazine, 2,4-dichloro-6-nitoxy L3,5-triazine.
この架橋剤の使用割合はコラーゲンまたはゼラチン１モ
ルに対し、通常１０〜１０００モルである。この使用割
合が１０モル未満では架橋物の物理的強度が上がらす、
１０００モル以上加えても０
物理的強度の向上が図れない。The proportion of this crosslinking agent used is usually 10 to 1000 mol per 1 mol of collagen or gelatin. If the usage ratio is less than 10 mol, the physical strength of the crosslinked product increases.
Even if 1000 mol or more is added, no improvement in physical strength can be achieved.
本発明の方法における塩基性条件下は、通常アルカリ性
の溶液系として形成される。The basic conditions in the method of the present invention are usually formed as an alkaline solution system.
このアルカリ性の溶液系は無機塩基または有機塩基を水
または有機溶媒に混合するか、あるいは水と有）ａ溶媒
との混合溶媒に混合して形成されたものであればよい。This alkaline solution system may be formed by mixing an inorganic base or an organic base with water or an organic solvent, or by mixing it with a mixed solvent of water and a) solvent.
無機塩基としては、例えばアンモニア、炭酸塩、炭酸水
素塩、水酸化ナトリウム、水酸化カリウムなどの通常の
無機塩類；あるいはそれら塩類のいわゆる緩衝液が挙げ
られる。Examples of the inorganic base include common inorganic salts such as ammonia, carbonate, hydrogen carbonate, sodium hydroxide, potassium hydroxide; or so-called buffer solutions of these salts.
有機塩基としては、例えばピリジン、トリエチルアミン
、酢酸ナトリウム、イミダゾール、２，４．６コリジン
などが挙げられる。有機溶媒としては、例えばメタノー
ル、エタノール、プロパノール、ヘンゼン、トルエン、
エーテル、テトラヒドロフラン、アセトン、酢酸エチル
、ジメチルアセトアミド、ジメチルホルムアミドなどが
挙げられる。Examples of the organic base include pyridine, triethylamine, sodium acetate, imidazole, and 2,4.6 collidine. Examples of organic solvents include methanol, ethanol, propanol, Hensen, toluene,
Examples include ether, tetrahydrofuran, acetone, ethyl acetate, dimethylacetamide, dimethylformamide, and the like.
本発明の方法におしする架橋反応は前記したコラーゲン
またはゼラチンと前記した架橋剤とを前記した塩基条件
下において行うものである。この場合、コラ−ケンまた
はゼラチン、架橋剤および塩基は一つのン容液系を形成
するが、この溶液系は均一であっても不均一であっても
よい。前記アルカリ性の溶液が溶媒として水を用いてい
る場合は架橋剤の水の溶解性を考慮すれば、架橋剤を有
機溶媒とともに加えることが望ましい。また、成形品の
コラーゲンまたはゼラチン溶液に架橋剤を加える場合に
も有機溶媒とともに加えることが望ましい。なお、コラ
−ケンまたはゼラチン、架橋剤および塩基からなる溶液
系では架橋剤が不均一であってもよく、そのｌｌ艮りで
は！彎、？蜀ン夜系を形成していてもよい。The crosslinking reaction carried out in the method of the present invention is carried out using the above-mentioned collagen or gelatin and the above-mentioned crosslinking agent under the above-mentioned basic conditions. In this case, the collagen or gelatin, the crosslinking agent and the base form a single liquid system, which may be homogeneous or heterogeneous. When the alkaline solution uses water as a solvent, it is desirable to add the crosslinking agent together with an organic solvent, considering the solubility of the crosslinking agent in water. Furthermore, when adding a crosslinking agent to a collagen or gelatin solution for a molded article, it is desirable to add it together with an organic solvent. In addition, in a solution system consisting of Kolaken or gelatin, a crosslinking agent, and a base, the crosslinking agent may be non-uniform. Kei,? It may form the Shunya system.
この架橋反応における前記したコラーゲンまたはゼラチ
ン、架橋剤および塩基からなる溶液系のｐＨは、通常、
８〜１１である。このｐ Ｈが８未満では所望程度に架
橋反応が進行セす、１１を越えるとコラーゲンまたはゼ
ラチンの変性を招き望ましくない。また架橋反応におけ
る時間は、通常、５分間〜２時間である。この時間が５
分間未満では架橋反応が不十分となる。好ましくは５分
間〜２
４８時間である。さらに架橋反応における温度は、通常
、０〜３５℃である。この温度がＯ“Ｃ未満では架橋反
応が進まず、３５“Ｃを超えるとコラーゲンまたはゼラ
チンの変性を招き望ましくない。In this crosslinking reaction, the pH of the solution system consisting of collagen or gelatin, a crosslinking agent, and a base is usually
8 to 11. If this pH is less than 8, the crosslinking reaction will not proceed to the desired degree, but if it exceeds 11, it will undesirably cause denaturation of collagen or gelatin. Moreover, the time for the crosslinking reaction is usually 5 minutes to 2 hours. This time is 5
If the time is less than 1 minute, the crosslinking reaction will be insufficient. Preferably it is from 5 minutes to 248 hours. Furthermore, the temperature in the crosslinking reaction is usually 0 to 35°C. If this temperature is less than 0"C, the crosslinking reaction will not proceed; if it exceeds 35"C, collagen or gelatin will undesirably denature.
本発明の方法においてコラーゲンまたはゼラチンと架橋
剤との架橋反応は、糸、膜、スポンジなどのコラーゲン
またはゼラチン成形品を架橋剤を含むアルカリ性の溶液
または懸濁液に加えて行うか、あるいはコラーゲン、ゼ
ラチン成形品とする簡のコラーゲンまたはゼラチン溶液
段階におけるコラーゲンまたはゼラチンの酸性または中
性の溶液中に架橋剤を均一または不均一に加え、ひき続
きこの溶液からコラーゲンまたはゼラチン成形品を得、
この成形品を前記した塩基性条件下に置くことにより行
われてもよい。特に後者の方法は従来の架橋剤がコラー
ゲンまたはゼラチン溶液中で不安定であったのに対し、
本発明に使用される架橋剤がコラーゲンまたはゼラチン
溶液中で架橋を招かず極めて安定であるため、コラーゲ
ンまたはゼラチン溶液の安定な長期保存が可能であり、
こ３
れにより実現されたものである。コラーゲンまたはゼラ
チン成形品を形成する前のコラーゲンまたはゼラチン溶
液への架橋剤の添加という従来の方法では実現不可能な
方法が可能となった。In the method of the present invention, the crosslinking reaction between collagen or gelatin and a crosslinking agent is carried out by adding collagen or gelatin molded articles such as threads, membranes, sponges, etc. to an alkaline solution or suspension containing the crosslinking agent, or by adding collagen or gelatin to an alkaline solution or suspension containing the crosslinking agent. Adding a crosslinking agent uniformly or nonuniformly to an acidic or neutral solution of collagen or gelatin at the collagen or gelatin solution stage of preparing a gelatin molded article, and subsequently obtaining a collagen or gelatin molded article from this solution,
This may be carried out by placing this molded article under the basic conditions described above. In particular, the latter method is useful because conventional crosslinking agents are unstable in collagen or gelatin solutions.
Since the crosslinking agent used in the present invention does not cause crosslinking in a collagen or gelatin solution and is extremely stable, stable long-term storage of the collagen or gelatin solution is possible.
This was achieved through these three steps. Addition of a crosslinking agent to a collagen or gelatin solution prior to forming a collagen or gelatin molded article is now possible, which is not possible with conventional methods.
なお、本発明の方法においては、前記した後者の方法に
おいて内部に架橋剤を含んだコラーゲンまたはゼラチン
成形品を架橋剤を含んだアルカリ性の溶液で架橋反応さ
せてもよい。また、従来の架橋剤（例えばグルタルアル
デヒドである）を含むアルカリ性の溶液で架橋反応させ
てもよい。In addition, in the method of the present invention, the collagen or gelatin molded product containing a crosslinking agent therein may be subjected to a crosslinking reaction with an alkaline solution containing a crosslinking agent in the latter method described above. The crosslinking reaction may also be carried out in an alkaline solution containing a conventional crosslinking agent (eg glutaraldehyde).
以下に、実施例を挙げ本発明を更に詳しく説明する。The present invention will be explained in more detail below with reference to Examples.
尖旌班よ
５％のアテロコラーゲン塩酸溶液（ｐ Ｈ： ２．９５
）を０．５５ｍｍの内径を有するノスルに通し、飽和食
塩水中で紡糸してコラーゲン成形品としての糸を得た。5% atelocollagen hydrochloric acid solution (pH: 2.95)
) was passed through a nostle having an inner diameter of 0.55 mm and spun in saturated saline to obtain a thread as a collagen molded product.
一方、架橋剤としての２．４．６− トリクロロ−１３
５−トリアジン０．１２５ｇをメタノール２０ｍ＃に溶
解４
し、得られた溶液をアルカリ性溶液としての炭酸すトリ
ウム−炭素水素すトリウム（ＮａｚＣＯｓ ＮａＨＣ
Ｏ３）の緩衝液（温度： ０．５Ｍ、ｐ Ｉ−１＋ ９
．２５） ５０ ｍｌに加えた。次いで得られた溶液
に前記した糸を浸消し、室温で１時間放置後、乾燥して
本発明の方法に係る架橋コラーゲンである糸を得た。On the other hand, 2.4.6-trichloro-13 as a crosslinking agent
0.125 g of 5-triazine was dissolved in 20 m# of methanol, and the resulting solution was mixed with thorium carbonate-strimonium carbonate (NazCOs NaHC) as an alkaline solution.
O3) buffer (temperature: 0.5M, p I-1+ 9
．． 25) Added to 50 ml. Next, the above-mentioned thread was immersed in the obtained solution, left to stand at room temperature for 1 hour, and then dried to obtain a thread made of crosslinked collagen according to the method of the present invention.
得られた糸は酸に不溶であり、かつ無色であった。また
通常の引張りに耐え得る機械的強度も有していた。The resulting thread was insoluble in acid and colorless. It also had mechanical strength that could withstand normal tension.
実ｌ烈童
５％のアテロコラーゲン塩酸溶液（ｐ Ｈ： ２．９５
）に０．１２５ ｇの２．４．６−トリクロロ−１，３
，５−１−リアジンのメタノール溶液６山Ｅを加えて充
分に攪拌して混合した。得られた溶液を０．５５ｍｍの
内径を有するノズ）Ｉｙｔこ通し、飽和食塩水中で紡糸
してコラーゲン成形品としての糸を得た。ついでこの糸
をＮａ２ＣＯＩ Ｎａ１ｌＣＯｚの緩衝液（濃度：
０．５Ｍ、、 ｐ Ｈ： ９．２５）に浸漬し、室温で
１時間放置後、乾燥して本発明の方法に係る架橋コラー
ゲンである糸（直径：０．１８ｍｍ）を得た。5% atelocollagen hydrochloric acid solution (pH: 2.95)
) to 0.125 g of 2,4.6-trichloro-1,3
, 6 methanol solutions of 5-1-riazine E were added and thoroughly stirred to mix. The obtained solution was passed through a nozzle having an inner diameter of 0.55 mm and spun in saturated saline to obtain a thread as a collagen molded product. Next, this thread was soaked in a buffer solution of Na2COI Na1lCOz (concentration:
0.5M, pH: 9.25), left for 1 hour at room temperature, and then dried to obtain a crosslinked collagen thread (diameter: 0.18 mm) according to the method of the present invention.
得られた糸は酸に不溶であり、か・っ無色であった。ま
た通常の引張りに面ｌえ得る機械的強度も有していた。The resulting thread was insoluble in acid and colorless. It also had mechanical strength that could withstand normal tension.
天４０４走
５％のアテロコラーゲン塩酸溶液（ｐ Ｈ： ２．９５
）に０．１２５ ｇの２．４．６− トリクロロ−１，
，３，５−１−リアジンのメタノール溶液６ｍｎを加え
て充分に攪拌して混合した。得られた溶液を０．５５＋
ｕの内径をイＴ−Ｊるノズルに通し、飽和食塩水中で紡
糸してコラーゲン成形品としての糸を得た。一方、架橋
剤としテノ２．４．６− トＩＪりＩＩ Ｏ−１，，３
，５−＋−ＩＪ ７ジ７０．１２５ｇをメタノール２０
ｍ１に溶解し、得られた溶液をアルカリ性溶液としての
ＮａＨＣＯ３−ＮａＨＣＯ３の緩衝液（濃度： ０．５
Ｍ、ｐ Ｈ：９．２５） ５０ｍｆｆに加えた。次い
で得られた溶液に前記した糸を浸漬し、室温で１時間放
置後、乾燥して本発明の方法に係る架橋コラーゲンであ
る糸を得た。Ten 404 5% atelocollagen hydrochloric acid solution (pH: 2.95
) to 0.125 g of 2.4.6-trichloro-1,
, 6 mL of a methanol solution of 3,5-1-riazine was added and mixed by thorough stirring. The resulting solution is 0.55+
The inner diameter of U was passed through a T-J nozzle, and the yarn was spun in saturated saline to obtain a thread as a collagen molded product. On the other hand, as a crosslinking agent, Teno 2.4.6-ToIJ II O-1,,3
, 5-+-IJ 7 di70.125g methanol 20
The resulting solution was dissolved in NaHCO3-NaHCO3 buffer as an alkaline solution (concentration: 0.5
M, pH: 9.25) was added to 50 mff. Next, the thread described above was immersed in the obtained solution, left to stand at room temperature for 1 hour, and then dried to obtain a thread made of crosslinked collagen according to the method of the present invention.
得られた糸は酸に不溶であり、かつ無色であった。また
通常の引張り乙こ耐え得る機械的強度も有していた。The resulting thread was insoluble in acid and colorless. It also had mechanical strength that could withstand normal tension.
実鮭は飽（
５％のアテロコラーゲン塩酸溶液（ｐ Ｈ： ２．９５
）に０．１２５ ｇの２．４．６−１−リクロロー１．
３．５− ）リアジンのメタノール溶液６用ｌを加え
て充分に攪拌して混合した。得られた溶液を０．５５ｍ
ｍの内径を有するノズルに通し、飽和食塩水中で紡糸し
てコラーゲン成形品としての糸を得た。ついでこの糸を
７％のアンモニア水溶液に浸漬し、室温で１．５時間放
置後、乾燥して本発明の方法に係る架橋コラーゲンであ
る糸を得た。Real salmon was prepared with 5% atelocollagen hydrochloric acid solution (pH: 2.95).
) to 0.125 g of 2.4.6-1-lichloro1.
3.5-) 6 liters of a methanol solution of riazine was added and mixed by thorough stirring. The resulting solution was 0.55 m
The thread was passed through a nozzle having an inner diameter of m and was spun in saturated saline to obtain a thread as a collagen molded product. Next, this thread was immersed in a 7% ammonia aqueous solution, left for 1.5 hours at room temperature, and then dried to obtain a crosslinked collagen thread according to the method of the present invention.
得られた糸は酸に不溶であり、かつ無色であった。また
通常の引張りに耐え得る機械的強度も有していた。The resulting thread was insoluble in acid and colorless. It also had mechanical strength that could withstand normal tension.
実七艷１し＼４
アテロコラーゲン塩酸溶液に代えてゼラチン溶液を用い
た以外は、実施例１〜４とそれぞれ同様７
に操作して本発明の方法に係る架橋セラチンである糸を
得た。A cross-linked seratin thread according to the method of the present invention was obtained in the same manner as in Examples 1 to 4 except that a gelatin solution was used in place of the atelocollagen hydrochloric acid solution.
得られた糸はいずれの場合も酸に不溶であり、かつ無色
であった。また通常の引張りに耐え得る機械的強度も有
していた。The threads obtained were insoluble in acids and colorless in all cases. It also had mechanical strength that could withstand normal tension.
以上に詳述した通り、本発明の架橋コラーゲン、または
架橋ゼラチンの製造方法によれば無色でかつ優れた物理
的強度を有し、しかも架橋剤の未反応の部位を利用して
染色などを容易になし得る可能性が期待できるため、例
えばカツラなどの用途に適用して極めて有用であり、そ
の工業的価値は大である。As detailed above, according to the method for producing cross-linked collagen or cross-linked gelatin of the present invention, it is colorless and has excellent physical strength, and furthermore, it is easy to stain by utilizing the unreacted portion of the cross-linking agent. Because of the promising possibilities, it is extremely useful for applications such as wigs, and has great industrial value.
Claims (1)
よく、少なくとも２つがハロゲン原子を表し、残りが水
素原子、炭素数１〜３のアルキル基、炭素数１〜４のア
ルコキシ基または炭素数１〜３のアルキルアミノ基を表
す）で示されるトリアジン誘導体、 一般式：▲数式、化学式、表等があります▼ （式中、Ｒ＿１乃至Ｒ＿３は前記と同義である）で示さ
れるトリチアン誘導体、 一般式：▲数式、化学式、表等があります▼ （式中、Ｘはハロゲン原子であり、Ｒ＿４およびＲ＿６
は同一であっても異なってもよく、Ｒ＿４およびＲ＿６
の少なくとも１つがハロゲン原子を表し、残りが水素原
子、炭素数１〜３のアルキル基、炭素数１〜４のアルコ
キシ基または炭素数１〜３のアルキルアミノ基を表し、
Ｒ＿５は水素原子、炭素数１〜３のアルキル基、炭素数
１〜４のアルコキシ基、炭素数１〜３のアルキルアミノ
基を表す）で示されるピリミジン誘導体および 一般式：▲数式、化学式、表等があります▼ （式中、Ｘは前記と同義である）で示されるチアジアゾ
ール誘導体よりなる群から選択される少なくとも１種の
架橋剤とコラーゲンまたはゼラチンとを塩基性条件下に
架橋反応させることを特徴とする架橋コラーゲンまたは
架橋ゼラチンの製造方法。 ２、コラーゲンあるいはゼラチン成形品またはコラーゲ
ンを含む生体組織を前記架橋剤を含む塩基性溶液または
塩基性懸濁液中で架橋反応させる請求項１記載の架橋コ
ラーゲンまたは架橋ゼラチンの製造方法。 ３、酸性または中性のコラーゲンまたはゼラチン溶液に
前記架橋剤を加えて溶液または懸濁液となした後にコラ
ーゲンまたはゼラチンの成形をなし、得られたコラーゲ
ンまたはゼラチン成形品を前記塩基性条件下に架橋反応
させる請求項１記載の架橋コラーゲンまたは架橋ゼラチ
ンの製造方法。 ４、前記架橋剤が２，４，６−トリクロロ−１，３，５
−トリアジンである請求項１記載の架橋コラーゲンまた
は架橋ゼラチンの製造方法。 ５、前記架橋剤が２，４−ジクロロ−６−メトキシ−１
，３，５−トリアジンまたは２，４−ジクロロ−６−エ
トキシ−１，３，５−トリアジンである請求項１記載の
架橋コラーゲンまたは架橋ゼラチンの製造方法。[Claims] 1. General formula: ▲ Numerical formula, chemical formula, table, etc. ▼ (In the formula, R_1 to R_3 may be the same or different, at least two represent halogen atoms, and the rest represent hydrogen atoms. Triazine derivatives represented by atoms, alkyl groups with 1 to 3 carbon atoms, alkoxy groups with 1 to 4 carbon atoms, or alkylamino groups with 1 to 3 carbon atoms, general formulas: ▲ Numerical formulas, chemical formulas, tables, etc. ▼ (In the formula, R_1 to R_3 are the same as above) General formula: ▲ Numerical formula, chemical formula, table, etc. ▼ (In the formula, X is a halogen atom, R_4 and R_6
may be the same or different, R_4 and R_6
At least one of represents a halogen atom, the remainder represents a hydrogen atom, an alkyl group having 1 to 3 carbon atoms, an alkoxy group having 1 to 4 carbon atoms, or an alkylamino group having 1 to 3 carbon atoms,
R_5 represents a hydrogen atom, an alkyl group having 1 to 3 carbon atoms, an alkoxy group having 1 to 4 carbon atoms, an alkylamino group having 1 to 3 carbon atoms) and general formula: ▲ Numerical formula, chemical formula, table etc. ▼ (wherein, Characteristic method for producing crosslinked collagen or crosslinked gelatin. 2. The method for producing crosslinked collagen or crosslinked gelatin according to claim 1, wherein a collagen or gelatin molded article or a biological tissue containing collagen is subjected to a crosslinking reaction in a basic solution or basic suspension containing the crosslinking agent. 3. The crosslinking agent is added to an acidic or neutral collagen or gelatin solution to form a solution or suspension, and then the collagen or gelatin is molded, and the resulting collagen or gelatin molded product is placed under the basic conditions. The method for producing crosslinked collagen or crosslinked gelatin according to claim 1, wherein a crosslinking reaction is carried out. 4. The crosslinking agent is 2,4,6-trichloro-1,3,5
- The method for producing crosslinked collagen or crosslinked gelatin according to claim 1, wherein the triazine is triazine. 5. The crosslinking agent is 2,4-dichloro-6-methoxy-1
, 3,5-triazine or 2,4-dichloro-6-ethoxy-1,3,5-triazine, the method for producing crosslinked collagen or gelatin according to claim 1.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP16915389A JPH0335000A (en) | 1989-06-30 | 1989-06-30 | Production of crosslinked collagen or crosslinked gelatin |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP16915389A JPH0335000A (en) | 1989-06-30 | 1989-06-30 | Production of crosslinked collagen or crosslinked gelatin |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH0335000A true JPH0335000A (en) | 1991-02-14 |
Family
ID=15881267
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP16915389A Pending JPH0335000A (en) | 1989-06-30 | 1989-06-30 | Production of crosslinked collagen or crosslinked gelatin |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0335000A (en) |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0385422U (en) * | 1989-12-20 | 1991-08-29 | ||
| WO2005054553A1 (en) * | 2003-12-01 | 2005-06-16 | A School Corporation Kansai University | Gelatin fiber and process for producing the same |
| KR100543220B1 (en) * | 2001-11-28 | 2006-01-20 | 호야 가부시키가이샤 | Thiol compound, method for producing the same and optical product comprising the same |
-
1989
- 1989-06-30 JP JP16915389A patent/JPH0335000A/en active Pending
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0385422U (en) * | 1989-12-20 | 1991-08-29 | ||
| JPH0527454Y2 (en) * | 1989-12-20 | 1993-07-13 | ||
| KR100543220B1 (en) * | 2001-11-28 | 2006-01-20 | 호야 가부시키가이샤 | Thiol compound, method for producing the same and optical product comprising the same |
| WO2005054553A1 (en) * | 2003-12-01 | 2005-06-16 | A School Corporation Kansai University | Gelatin fiber and process for producing the same |
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