SK160391A3 - Recombinant proteine joining complex viral antigen hiv-1 - Google Patents

Description

Oblsat techniques

The invention relates to a recombinant phosphate protecting agent, the HIV-1 viral antigen. a state of the art

The human monoclonal antibody (s) is characterized by an immune response against astlgen obtained, for example, by B-lymphocyte cells, and by B-lymphocyte sclerosis. Wortalize the fusion with the appropriate cell lines, the myηίοκι myηίοκι omuηίοκι omuημικοomu κομικοatoato (získané) is obtained by obtaining the hybridides, the hybrid of the axis, as the production vehicle pro for αAK e, Mokcu s Use in vitro in multiple business cultures and cultured in the need to 'measure & u / Grtrnow, B " tfahn I, " S " " X * fi " H · BtelnSceller 9S " , S. ^ aitanovieh, 1 * GOrtler, 1 '· JDetnhsrdt, H. Sati nger, and H, von 2aehr, l $ 8 $. The higbifluorophenoxyfluorophenol (II) orthoclerophospholefin is CE-FT (3), imidstol, x-amide (106) and (257). As a rule, the fabric produced is a rigid material which is made of a tubular material and 2 lightweight elements which are mutually connected by a drill screen & together, specifically forms a vase of antibody / Wateon J.B, H ϋ · Hopki: no, clay · W.obiob®, J * A. Gteitz and A.M.'Eeiner, 1937, Molecular Blology of the Gene, Vol. 1 and 2, Xlie Benja -in / Cu.oraing © Coa-rany, Ino. / ·

Gtruki ^ aa such antibodies can be divided into a constant region (s) that is responsible for the so-called furxic, such as, for example, the < RTI ID = 0.0 > a < / RTI > which antigen.

Antibodies la © étépít ensyoatioky bioohôxaiokýci

vv

From thod & rai. E & d e r e r e r e r e r e r e c a d e r e c a m e c a m e r e c a m e r e c a m e r e c a m e r e c e m e r e c e m e r e m e c a m e r e c e m e r e p e c t the ability of the relevant angigen to be analogous to Yak at the original antibody / WataontJ!! * SE · Sopklne, i *% Y iobob, d, A * Steitjs end A * fo · & elaerflSiä7 Molecular Biology of Tl £ e, Yol · 1 and 2, Be'eyatsin / Cusslcg rubliehiog CoupAy, InOf prote ol ol ol ol ol ol ol ol v v v v v v v v v v v v v . Neither gdcleks nor reproodulating 2a 5a to uaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaaa/) site © within the mift * hl © pôrtior.s of fever ani ligfct chaine, Proo · Kati · Aead, Sci * USA 6 < tb > 2659-2662, Eoe5i®aK; n # š ·! > * Inbar end Q. Givol * 1973 · An activa antibody fragment / Fv / oompoaed of tha vari, a portions of i-avai and light ohains9BiocheItions 12 i 1130-1.135 / · i-omooi method gene technique but it does produce Fv reproduc fragments & telnč · This prerequisite is already used by &

With the help of the routine, oDIA produces a cell hybridoma producing with the Ac 2 hybridon producing ®Ak and isolating all HKA.This KKA contains the ribosomes of BSA total anoletvl transcells. How Nodind Inducted Nuclear Thorns Them, How Them ThemAppoplasmatic Throttle, So Announced, aeeeengr MA, Cheese ae wg & at the end of Y, this poly-oligonucleotide and at the same time the affinity of the γ-λ-UX-o-cellulose is scanned by a λ-axis, and the β-" Use HEA to overwrite n with the oDM · Using appropriate scraps, you can clone, leading to. so bruise the cBM boar ·

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known. ' imurog ± o du ± genes c e'Data library, Eeidelberg, ESE /, can be confident about identity. In this way, for example, cations bearing a light or mAH sequence are isolated. J '‘·'. By analyzing the sequence obtained by this method, they can be identified by comparison with the known compounds. if the single domain is also single domain. -: a. skull. .fetézeé j 'i can be identified: variabil-vHĺ ä constant region, and for example inside? variable region so-called "hypervariable n regions" or "quot; no-gion ^^^ which is; self-reluctant viral binding of antigen. / Kabat · ÍI > I ·. · Wu. ’. fíeí d-Mi; ller, Ε.Ιί. . Per r y and K.S. Gottésmann, $ 1 37. ^ S u q q £ prot prot q q q q q q q q q S S S S S S S S S S S S S S S S S; In this way, the genes / genes of the present invention are different genes for the expression of different genes. Use. on the one hand, animal cell cultures such as mouse cells can be used when suitable expression vectors are used. [Heuerger, ls. 19S3, Expression and regulation of heavy chain gene transfection into lymphoid cells, KZEEO J. 2: 1373-1373 /. Use of yeasts / iveTood C.H. II.A. Boss J.H. Henten, J.E. Calvert and iť.A. Eoberts, 1935. ihe syntkesisand in vitro. assemb.ly 0f funktional antlbódles in yeast, Hature / london / 314: 446-449 /, or bacteria cells /Boss.M.A. J .A. Henten, C ..., V / o and J * S. Em tue, 1 $ 34 * Assembly of ftx & otloael antibodies to irasanoglobulin heavy and length efcaina oyntheeloed in B * ool f Eucl * Acids ®e * 2J 3791-3206 / as an expression vehicle for complex antibody problematic ? ® ns d d d d ná ná ná ná r r r???????? oval oval oval oval oval oval oval oval oval oval oval oval oval oval oval oval oval oval oval oval oval oval oval Transfers of the antibody in Belá © urokarycncch case of prokaryotic * Mlβ are described by four phthalene ethers which allow the expression of Fv popFib & Fsb fragisents in Bach® · riekla ooli # 'B'kerra e Hfcclktbua / 163 * Aesenbly of a fasetloaal Immunoglcbulin Fv < tb > ______________________________________ < tb > ______________________________________ < tb > ______________________________________ < tb > ______________________________________ < tb > Bacterial Leadership But For the Proauktd to Peri · Plesunatiokéh Bacteria Proof · IM too ee is le & dr protein A external mmhrénj / cprsA / its δ i alkaline foe · fatasm / phoA / · After tranafekel this plaomide to Beehori * ohla coli has been shown to express the antigen binding protein in bacteria free of bacteria *

Bctier © al * / Better! ≫ F, Cbarg b.F. Kobineon and Λ * Η * · Horwits 198S · 2soherichia ecll secrebion ef and acuivivabi? Ri ri í body body body body fragment fragment ion ion ion ion ion---------------- in which the identification of the ganglioside antigen is often carried out on the surface of the human cancerous cell line, the conjugate of the present invention. does not become Sal promoter. · TOnelv typeMouriuv β * βδ, like yel, B Ieg3 or sequence always tuft ecodes coding with p streams totinone · 2 pvxv.tversions cours trs, m; " 'ornate eh. Bacteria Fragmenting Antigens *

Charts a: BlUckthun / í ^ Now: ^ · is'erably :. o f - a; , .f ime t ional immuno giobulin? Fv, kr ägment in; E s -: ^ é ^ x x ia ia ia ia ia ia ia:::::: b b b b b b b 38 38 38 38 38 38 alv = ~ c y δΐβ-ΐΐώ'ι »lf. ifeíÄSiií’er 'l? -v: -: P' V'-ÍPAíί · ^ 'ϊβ ^ τι? ·: βΓ < Λ'- Δ ť Ό

rriessenger Eli A is a piece of information for both ex-adherent babies. Authors. indicates that this is done by pro- a sulfuric acid additive. Polypeptide, which extracts the base for accurate, continuous placement of variable. the region of a small chain yVg / with the region of light koe- - - ;: T. kBross. .this problem, namely creating a 3hr " heterodener / in nature non-syyloyaline yshazan / se-trough:: Huston et al./Huston J.S. ;; D. Xevinson, M. Mud's get. J. Eo'votny, M.U. Margolius, E, J. (Bidge, E.E.Jrucôoleri ,. · E,. Eáber £ Ŕ. -Crea and H. Opper -r; / fsi ^ hV ^ i'S38, lrd iein. engiňeeyingi o íksňtiboďy .. b indíng site s: '' r • r.eďoyéry of spécifip aotivitý in .án. aati-dioxitx single. chein Fe analogue in Scherichia coli, Proc · Kati. Acad. · &Quot; ^ bi > IJSA: $ 579-5.233; et: al * / Bixd, B.S.Z.D. Bard J.W.! Jacobson, S. Johnson, B.M. Kaufman ,. S.M. lee ϊ >: léé, S.E. Bope, gs. Eiordsn and M. Whitlow, 1988, rtSingle-Chalir. Antigen-Blnding Proteins. Science 242 with 423-j. 426: another method, namely, the coalentric, by linking the linker to the amino acid linker that does not occur naturally. This linking sequence is characterized in that it consists of a certain amino acid equivalence, so that the gap between the naturally occurring regions of the region between the regions to be bound does not occur in the natural conjugate. conformation has led to unnecessary stress.

Eusion et al., 1933 Protein ehgineering of antibody bindings: recovery of specific aotivities in anti--6-, dlgoacin Biasgrle-efcain Fv analogue In Esoheriehia coli

Kati * Acad * Ss.i U.S. Pat. No. 5,175-5333 / opposed variable regions to multiple digestive antibodies to help ηρ® $ β «, MKfla 7etf2C " 15 " asdnokyeelin sekves.ee 3GGG3ÔGGGSGGGG3 / «Configured was a Vg-línker-V ^ · Xento single-fetus eiogle-ôléia-Iv ngngcieat / Fv fragment was cached in © Mís Xeadex and controls of the ethic trp-promoter / operator are shown in the following non-limiting examples of their respective molecules in EC1 containing guanine. the side of the woods of the cave with the hydolyolysis is in and out of the wood and in the graph and the graph 1 of the footsteps of the stone and the grass, the simple bark / aisgl * - ohein / Fv fragment that your © antigen * one of © spSeobÔ. in analogy, was approved by Blrdem et al * / 193-3 * Single * Chain Antigen-Bicdlng iro - · teins, Soianoe 242 s 423-456 / pro however, the pH of this protein weighs the sphero-phiotheoresin, but the 13-amino acid line was used to immunize the antigen, but the 13-amino acid line was imaged by IICC3VSSEQ14QKH31I). Sentfr linker j & eti of the huoáani " earbonio auhydraee ** and was exiled with. 3for the acenacean database and the tractor, the structure that fits into the amino acid position of the amino acids Fv rag sta sta sta sta á sat sat sat at u at u u u u u u at at at at at at ./ 1933 Terry cloth in bindings and bindings in a specific type of atypical in an anti-digexin adagie chain IV & loyu © in Macherichla ooli < tb > sr · V ^

Acnd Soi. UàiA &£; 5379-5TO / · for geafl. for the production of fragments in the ascolhera colt 3, they are sampled in one case, or in one case, the barrel or the pellet is plated on the cheese / lyophilisate. 7

Fab% / Fab / g and Fv fragments occur in comparison with the coreplein antibodies, the intrinsic entrances, and consequently, the antibody-mediated antibody antibodies and antibodies. e, quicker difonding even in the case of even. the application is in operation and the reason for this is more controllable, and in the most important way is the pH of the pH of the essential xegieml (e.g., & efekiorVf vaaba n & the receptors and the molecules of the receptors are not unconscious or even disadvantageous, they are. the following sections are valuable * or *. For example, using kotsplet antibodies, the pH is subtended to the tumors of the problem due to the fact that the specific signals are placed in the subsoil of the undesirable virus-free antibody. entft, lodle of this can be used for the application of the present invention in a simple process by simple pH control in the tomography of another medium (Blrd et al., 1988, S.I.l.). '' hain, | tet iger ^ Bindlag Proteins, Sceonce £ 4,2 t 423 · 426 $ Hustom ot al «* · 1903 Frotais angina © ring or antlbody biH · ding sito« t recovery of f? peeífio aot.1vi.ty in an anti-di · slngle-oh & in fv oxi & logue i »Jteofcpr5 cfela ooliti'roo ··

Aeed. The USA has 5379 * 53.33 water which, in its own right, has a low molecular weight water formed by N; i turn :, '^ <' íl r > Tr M *! óvnf lá > ko /! - * 501 oku * 1 ^ yv A *. Most likely, the antibodies and antibodies have been treated with antibodies, small and small-sized antigens, as described above. and jak as ige ige ige ige ige ako ako ako ako / / / / / / / / / moleku moleku moleku moleku moleku gly gly gly gly gly gly gly gly gly gly gly gly gly gly gly gly gly gly gly gly gly gly gly gly proteins and polysaccharides, & flowing out-olak-rary · o t a. The ship of © exalso contains the protein of the aforementioned region, the regions of the antibodies, coming from the pd, the © p · -3 · S.D6 / Aoeesiort 6 * 37110301, PEIS, Norton Bown, Μ / Grunov et al * f1333? to bigheffloioncy, feuimn B o © ll isanorta-lieing hoteroayelom CS / S7 ·? js IjsquccI, Kethods 106: 2571 DSpel S, B * T * íortíE & rs.Ii. Grúne v, A. Ounghaiissr and K, v * Baefcr, 1 $ 3 $ * Appiicatior of aunanal acnoelonal antibody ln a rapld ccsrpotétlve -Hnit-EXY BUŠA, d, Zannoel · »4ethode 116y 229- ^ 33 i Wpel, 3« S * B «Yorst« enr, f P. Eenklein and S. von Baehr, 1939 #H »e mepping of au ffisunodoao & ant region ef the tranaJBOrabrana protein of the Buaen lamraodef leieney Yir © / HIYil / by diierant peptidee end tlielr uae in anti-HIT ulieiuJ · Virol. Metb, 25; 167-173} Jungbauer A, 0 * íauer £ · baniach,?. © lt ér ér ér M Ut © © M © © © © © © © © © © © © © © © © ai ai ai ai ai ai ai ai ai ai ai ai ai ai ney Yirus BIY-1, 3 «EiQohoa ^ Biophya * Metlu 19 / 2-3 /» 1223-240, which are beating. antigen, it is firstly found in human or origin origin, which satisfies the desired property and which is also resolved in the 3-bottom cellular body as the kva. and in k & The present invention also relates to the manufacture of simple photolytic constructs derived from human antibodies. On the other hand, the easy-to-use capsule is disposable. vysokosíolekuláriií. Contextualization of the Viral Antigen at το < ί3Π from. the best * well-defined entigonds * 3 © could be seen 8® corresponding to the fret & gwentd ' s simple < tb > For example, these antigens include, but are not limited to, the antigen molecules, such as those in which the number of amino acids is n & The mixture was stirred at room temperature for 10 min

Similarly, for example, an antibody to the antibody is present in the antibody antigen, -9- / tolerant &

It proceeds from the cellular lineage that produces the IgO1 / kappa-type ooclonal antibody that reacts specifically to EXV-1- p41 and extends to? í Sova recrea- © i ô · 1-, δρ1 £ 0/3 ^ 6 / | / Štúrov li.Š,, 0Ehn s, 1-oretroann, S.2 * Ki® © Bíng, 2 & · Steinkoll © r, .PeäteJ.Rdl, JD * Kottanovich,, 1, GUrtol,!; '· Seiiihardt, J & t Katiuger & !, von Baehr, 1938 The bightyxi noy ^ huinaii B oell ivmortAlidag heterony -. &Quot; elOTsa CB-17, J. lawunol, Method 106 with 237 and DCpel et al. 1939 »Applioetioc ufa humgxi monoolonal t ntibed in a ra id l l l l l----L L L L L L L L L L L L L L 1 1 1 1 1 1 1 1 1 1 1 of axt 'Imstraodo -sdnant region of ih® tr & rr * aemferan © protein of tbe Kumen Im ^ unodeíi elenoy Víru »/ HXV-1 / by clíffer & nt peptid © and the anti-HIT < ·! . E1I3A, f. Vlŕol * Meth, £% | 167 -17- i .Jm'glfcuer ©: t el «, l $ -39 · Xiloi daale fxoduotion of a £» $ «*. áraroclonal Afitihody Äg & iaot Sutsan lic: tucoá®fici © noy Vír? , by Pi-och. © ® · - Eiopkys. & © / 2 * 3/220 220-240 ty ol ol ol ua & & & & & & & & & & ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® ® 21 21 21 21 21 21 21 21 21 21 21 £ 21 aetbeda guan d.in-i * othlokya & rol Stá? 3.7: ¾ 0301 / darila, tie e t al. 1, 2, 3, 3, 3, 3, 3, 3, 3, 3, 3, 3, 3, 3, 3, 4, 4, 4, 6, 7, 11, 11, 13 In the present invention, the present invention relates to a composition for use as a substrate for K i. t, f and * jťhaaraaoia, 'Sweden /'

Cloning b’ *nA toru pUCl · · SokoisbJ%% otr.y to iSseheriokia 0011, media / 8l8 © t & 1.. u® performed in plasmid vein, and even the placenta was? trnnsforia - hr * sn © 2B1C1 and cultured in X® I932, iolocular Cloning and ha 10 boratory axSaxmal. , Gold Sprlrxg Har "York, York | Sold Sprirg Earbor lafcaaétory / *

The torsionary gems to and from the cybridis & ee and the o-daxi epeoiflucid for the oligonucleotide " Sekyas.com for eoody " were removed in the datotoano DMBX IsSA eeconv. popM ^ -ads to & ppa • skulls. četézed *

The jewel-identified < RTI ID = 0.0 > hybrid < / RTI > hybridase signals were further characterized by roatx analysis and were identified. fictional those clones # which n * sou plas-ssldy and «© .idelSízui ínoerty *

Skakvandn-f analysi tlehto kloa & have the idioms and coding of the region code been identified, namely vftdy po ^ adnoa kloiro · for t-ftkj? in the case of the skull chain of the antibody, the antibody was treated with the compound of the invention in the form of an antibody of the formula (1) or (c) of the formula (61) (S-EQ 20: 2). ID r P ubject obrd.gk ·! nft rendering ‘The invention of hu * bl g g * * í S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S S.. cbr * 21-y. 1 '•' at; < .ce na- · ρήαο1οό.υ. the fusion region and the variable region of the antibody region 3 ovaná 6 / £ Q Q I í / báze báze báze báze báze báze báze báze báze báze báze báze báze báze báze báze báze báze báze báze báze báze * ované Ny uvedený ou ou ou ou ou ou ou ou Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is Is UBR. 2 * í Mutec © na. pf-trade mesi -variable® region »and constant rt region® t C Sk oho antibody chain 3D6 / 33SQ 12) SO1 / · Mutated b · s® oansafteny * * * · Codova · n-// omluc-ly & In the wild-type DM, and in this case, there is a list of reatrics. BetsBl inserts the mutation.

It is the case of the "loadrc" and the "loadrc"; w'n / * region »ä · vertaMlnfw region® the lightweight antibody chain}} β'β · / 255Q ΙΓ 'SO: 2 / · mutated bizQ isou Denoted by * Jf * · Κθ · dovaré amino acids ^ uou listed in the wild type DSAfkxoifié Λ * 11— '- - 11 * 11 -' - - '$$? W - t $ & & · ^ ¾ ^ ¾¾¾¾¾¾¾ ^ fí ^ ofco? ^ Share the quotation x £ stá $ | · vamvainiclá · " '

as the 7 ' -codone of TA A. / -yanein-iu, - .beta.-BKA sequence linking the VE-linker site before and after the mutation to reproduce the amplified amino acid sequence in region VII region (SEQ 133 HO: 3). Kutované. bázevjaou tagged. . * s " The final sequence is shown. arji-; / ^. iípky3e, iiny ",: /. ': / -; , '··· " FIG // ,. 6; The BKA sequence of the linker ' s linker " VX ", and the linker ' s linker ' kséliny.v óblasti. \ X; iuegioriu / SEQ-I2D; KO t 3 /. Mutated. , bases, are denoted μϊ w. Is the final sequence of the asino- · · · kyq ^ lXny .-; .// · /:./;'- '·': v Λ. ', · Rnjbl

OsBs / gelcellback: sd3D6. Molecular weights / pbb of the standard are given. westeŕnjblotý "f:;: ./ ·; /// óbr v 8 / t / IiIV-T / prdu yards b ané p? or antigen-binding protein: 1. sc3B6 protein. '/ · - · · -: / second APso3B6 £ narrow protein (? 4? 3? 3B6:? 4? Total protein from L. Coli Fig. 9 · shows the KTV-1-antigen deficiency in the standard curve and that in conjunction with the se3B6 protein,

Fig. 10: Composite EIIIA assay with APsc3B6-protein. The sample to the right of the lace is a serum negative for EIV-1. Examples of Exemplification 1 7 selector insert of pUC3B6KC / SEQ II) HO: 1 / after 12 case Γ'ϋ03Ι) 610 / 3.2¾ ID KO : 2 / ifteatifiated by pfe - luncheon the regonon le & peptide and the var labile with the variable region and the constant region. gionic acid, polyolefins with phenylenediophenols. vilro vmt & genoaiei 8yeteatAtsersshaa UK / fcyly on this one, the shecfc has been converted by aaaldtajoí «atae® / visa oTji» 1 • d / # T * Mutaoi have been introduced in? recognition / ideati · f * cv®noe for certain resirifc & $ uy®y «ΙΟΏβοί trehto r®et :: - ivà'r,. The antibody and antibody codecs of the present invention may be subjected to a transducing plasmid, and the codon and stop codons of the present invention may be included. © xpreoi. The two oligomeric regions which have been formed by the two bifurcations of the two oligonucleotides have been avoided. and © together hybridize to < k > ', a double ' ', f ' is formed at its ends, there is a plurality of sub-regional regions which correspond to the same. .pľ- © Sr., fvaj £ Eis! what sucks that even the fetishes give? I have to re-litterin my dreams at the level of my dreams. restr © restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr restr............ eas; is & ·

Viséjcr-nou Xigaeí 3 suitably forward & The purified fragments of the genes which are located in the gene that are labile to the labile region are labile regions. .llr & erCB nael. there are some goods and restriction sites that contain ruccides. This is the same as the 5-thirty-five-thirty-five-thirty-five-thirty-five-thirty-five-thirty-one.

In order for © to reconstruct the original saplings © - asinbkyeelibynylany listed transition points to produce no ·

" .. Mò in ... m .DEJI / óbr; · 5 and 6. / > &Quot; .'ľ ".IN; , that is, - trudván · gen ^ kierá, ·; .... V g ** li2ér-T-. This engineered gene. s é. o

is labeled pGOsc3D6. ϊ'ΟΧΟΟί thť.:. t | 'has " the structure ...... í * 'sc3D6 gene th X is calculated from the plasmid p * JC £ c3D6 by r e-. . the enzyme sequences and inserted into the bacterial or expression vector pXZ223-3 / Ph & rmsoia, Sweden /, which contains a tac-pomot, an irradiated isopropyl-β-tertiogalcoid with IPTG /. The bisecting virus is labeled p £ KSC3D6 and was transformed into Esteriehia coli strain JM105 ·

Balloon culture

The transformed bacteria were cultured in a laboxator fermentor up to 0 ° C in a laboratory vial. (Ianiani et al: 1982, Moleculas clonins, A. iaboratory Manúal,-old- Spring Earbor, 15ew York :; Col & Spring Earbor la-; boratoří /. Expression was then induced by the addition of tert-propylthiogalactoside (IPTG). The bacteria were cultured for another 3 hours in the presence of IPTG, then harvested by centrifugation and stored at -30 ° C. Then the protein was extracted and you. -cleaning.

Extraction and purification

For each test batch, 10 g biomes / wet product weight was used. Cells were lysozyme-lysed. Frozen 1st coli paste is broken into sheets and prepared with STE buffer (10 mM Tris, 100 eDI KaCl, 1 mM EBTA, pK 3.0 / 10 µSuspsns1). A mixture solution containing nucleases, lysozyme and inhibitors (see Table 1) is added to this suspension. This. suspension with e. 2. coli is incubated for 15 minutes at 42 ° C. The addition of lxiton-X to a melt-100 (final) concentration of 0.5 l / well and at 42 ° C lyses the lyses. ♦ «* 14 · ♦« * 14 · ch tíTísek

XkUze -j í i '·' *: 1! and t 36 a * c-s: 3τ · · Γ..ξ ηΐδ in zib buffer and B h f - ^ c · t: Uzk & & e will enrich your oaet * edfiiiia.To < * vl.a% -G α, from & llvkcv ^ c}. «K.uMavek vcese < rIvcerirjov ^ • c r ;: f · /: ·· '· - > c! 3 csrir. / f o3for »Ônar.ov <ŕ-;; ip uf ru / ihoepha · ^ jsu lered 0¾] íre /» 'BZ // 9 prevratvf sts.ir. ^ n objarnom aue * p ^ r-ss and -clean / 3a s:; tnat, 6000 oVsic »4 ° C, JÄ-2C · rovor, 22-21 -a« t? Aáivkft # fy Beekruarm / ·

KozpoySt ^ f Ink) u. ; Forums t /, ÍBf > k

The difficulty is to dissolve in 6K G;

/ v ~ xr > «F to- ^ hj or 1 ú a / v H? 3, pil 3.3 »« and pH ** f Λ > '' -f? * '** / * Seter: o e let e no river determine the content of px * o »with e5-u.

Ka.fcld: r-g ·

In the present invention, there is a preferred embodiment of the present invention in which the compositions of the present invention are subjected to a process for the preparation of the compositions of the present invention. .i? -‘M t sk? ≫ & and / or for the protein / iiHuClCl S ;,, liuRtttococ d d 30 30 30 30 30 30 30 30 r t t t tatat at glutatatatatatatat 3 3 3 3 3 3 3 3 3 3ififififififififififififif u u u u u u u u PB PB PB PB PB PB PB 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3ififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififififif # Vor.o ^ ntraoe Sia £ ^ C ii, ·? protaíou /.; i - 's: r! 2 3 * 0 po. c ôr c it it it it it it it f f f f f f f f f f f f f f f f f f The solution to survive for treatment. ¾ e; pho 37 ° o works. £ '•' • tne * po sk! ···' :'::::: :ooooočíčíčíčíčíčíčíčíčíapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapaapa. torr 'S i o / re-rs fax-i «2 a. t í and «δ 1 by 3 y Qdeb.v *? ny vrrox. pH byle sai-trivsija to 't' to make it easy for you to do it. 3 d I c a n d e c a d c e rs have been fed to the DSBt, the 4700 rpm IC, the temperature has been filtered / pumped 0.02 ua, lion; rroiuítn- b b -.- j’r.g /, v p? The need to do this is done by gkpn · 'c on the order / © 3 ipor ·, etol. 250 µl of the olefinic analyzer Hlfl < C with the phase f, iSuoleoell 300.5, 4 x 125, f and 15 were analyzed.

Macherey and Vogel, KSK // # linear line 0.1 $ ΪΡΑ / aoe -tcnitrll 10 - 60 £ set up in 40 minutes / ·

The developed so3X6 is ultra-dialysed using 1000 dalton eutoff polysulfone membrane. The diafiltered protein solution is applied to the anion exchange and then eluted with ICO ® M EaCl. The so3U6 is deionized by gel filtration with Sephadexet G-25 (and Pharmacia, Sweden) and by the eta-gel method. / Eakanc P.E. and A · Eawaol, 1974 Peroxidase labeled antibody: a new method o f oon ^ igatloo, J # Eistoohem · Cytoohew., 22 t 1084-1091 / conjugate with alkaline phosphatase

The purified ec3U6 protein was checked by SPS · 6A6 / / Fig. 7 for the functionality of the U3 66 protein was performed by a tetramer alot assay with -17-1 test strips (BioE & d, USA). As a positive control, an analogous assay was performed with the transferred antibody, isolated from animal bovine cells.

As a negative control, preparae veer was used for -teine with E. ooli. The result of this test was & 3 ® is known from FIG. 8 *

Protein bo3U6 protein rotates affinity chromatography with a suitable purified 31 protein by producing standard Freund ' s adjuvanted rabbit oerum conditions. Pharmacia, Sweden) IgG fraction was obtained from rabbit serum. The antibody elasticity was determined by the Bli-ea assay. The 15 amino acid peptide (GGGGaGGG-G3GGGGS sequence) was prepared using a peptide synthesizer and then conjugated with a carbodiside condensate with a bovine albumin serum / BSA / molar ® poaertt 6i. Microtiter Plates Coated With Three Twenty Twelve Tulle Sera · Serum Sample was incubated in coated acroprotective decks and bound antibody was detected by peroxidase-labeled anti-cage-16 Ιΐδίο IgG. The so produced and cross-linked g, nti-so3E6 was ligated to sepharose 43, activated by BrCE / fa. PHARMEC & ff Sweden /. The bound material was purified by extracting the so3B6 protein which was, as described above, reprocessed and deionized by Saphaeox G-25 / fa. Pharmacia, Sweden was loaded onto an anti-So3-Ώ6 column. Unbound material was Vyrayt and specifically < RTI ID = 0.0 > < / RTI > So3I > 6 protein was digested with 0.1 M glycine-ECI buffer, pH < 5 >.

The electrophoresis was verified as described above by SI electrophoresis, and its functionality was tested by a Western-flotated test line method for the immunoaffinity chromathography of [alpha] 3H6 protsin is the following: with the help of Complete's Preund's adjuvant made by rabbit-sera. The IgG frakoe was profitable by GK sepharoae Fast Flow, and the phage (pharmaola), to make the anti-BSA antibody. The thus-obtained anti-linker IgG was coupled with Ecepharose 4B activated by BrCE / Ba, Phar-sacia, Sweden / * P * purified extract of oo3D6 protein, which, as described above, was back-loaded and deionized by Sephadex-G-25 / fa Pharosoift, Sweden / was not - dream on arthi-linker slcupec · The bound material was ours, the specifically bound so3B6 protein was eluted at 0.1 2 *! glycine-KCl buffer, pH 3.0. Subsequently, the neutralized IM Tria buffer was eluted and the sc3E6 protein was identified as described by SBS-elevation and Western blot testing for functionality.

Irunoaffinity Thrombotic HIV-1 Gpl60 Threshing

For the production of 3B6 isunoaffinate column, the di-protein was bound to 1 ml of NES column / fs. Pharmaoia, Sweden // It. protokl. fa. Pharmacia /.

4 ·

; Vj · O f & '' " '/' iysib - b f'-i viruses 5/2 /: 159-171 /. cpmbimat. - derived liIY-1 gpl60 an''-aha ·; - and £ nn »än: Iietró« hh. h ·· / · v. * · '; The invention is based on the following examples for the amp; in / l ^ V-l, which. &Quot; is. " ee ee ee3D6; 3 ^ 67 ^ 5 - ^ - 0 e i3D6; prc > - ·:; t0iEiera ;; '^ l3yIa4pri ^ ea:' by Barreta et al./ Barret NA · j; ; H.C i. Pallo 'a' · E.'Doxner * · 19.89 · Large-scale production and purifieation; The purified material containing the recombinant gp1S0 was concentrated by ultra / diafiltration and conditioned for the incruroaf initially sc5b6. This branch of ionized material was deposited on the scaffold and sc326. Like. equilibration pn.fr was used with an iris buffer pE.7 → 4 with 0.1 $ >. The tween-20 antigen was eluted with 3 M rhodanide. The yields of the individual grades are summarized in ta · bulee 2. ·

Example 2

Other cloning sc3B6 ,. in which the sc3B6 gene was a fusion of the alkaline phosphatase (EcphcA) gene isolated from Escherichia ci, the following was performed: the sc3E6 gene was cut by restriction restriction from plasmid pUCsC3D6 and inserted into the vector pEcphcAMut3 / Kohl, JP * fittker, B. Eimmler D. Mattanovioh, and H. Katinger, 1990 Enganeered gene for. Escherichia coli alkaline phosphate-for construction of translational fusions, i: ucl. Acíds Ees. 18/4 /: 1069 / The exiting vector is designated pAPsc3E6. The vector pSephoAKut3 contains an alkaline phosphatase geh isolated from Escherichia coli / Shuttle-v / Dth: Jylorandand III. blinton, 1936, Sequence of the gene for alka · line phosphztase frosí Escherichia coli ji > 133, kuel. Acíds Ees. 14/21: 3639 / did not contain a cutasease-directed oligonucleotide that was restriction in place of the end. This is a region that allows the ScphoA gene to be conjugated to another genome. by the expression of the fusion gene

; '.: νν ··: ν: -v - ·. .. ...... ·; '··,. - · & Cs cs cs cs cs cs cs & & & & & & & pla . The SEID pKK? Jscsc3? 6 was transformed into Escherichiae and the strain JP105 and the transformed bacteria were cultured in the laboratory in the medium of J? Aniatis et al. 1932,. Colecul & doping, A Laboraiory iLanuai, Cold Spring, Earbor New York: Cold-Pring Earbor-labox & following inactivation with the periplasmic GPTG-b1 active EoPhoA-sc3D6 fusion protein in the native or bacterial compartment, the following is purified: " " reaps. centrifuged and washed with iGrc. Tris buffer pH 7.5, supplemented with 30 mM EaCl. the washed bacteria were resuspended in 3333 ml of Tris buffer, pH 7.5, and added to the solution; The pH of the buffer and the pH of the buffer is 0.1 [mu] g. After . . After 10 minutes incubation at 0 ° C, the inhibitory solution was added, which was then mixed and incubated at room temperature for 10 minutes at room temperature. from PMSP and EGTA. &Amp; The bacteria were centrifuged. The residue was adjusted to 115 mM Tris with a final concentration of 25 mM Tris. By this process, the periplasmic space SbáÝ BunéklE. coli

By blasting off at 1200 g, the protein rc-c is cleared and then concentrated by ultrafiltration ·

EcI-hoA - sc3D6 protein is further purified by hydrophobic interaction ientov, cromatography. Ploví / fa. xhartnacia, Sweden ./ by la ékvilibxo v éna with 5C% saturated solution of arsonussuate in 23 eM Tris pu -fru pII 7.5. Protein solution b-1; equilibrator / column / column buffer per column. Sc3D6 elutes with linear gradl-entera 60 ý > ammonium sulphate to 0 $ ammonium sulphate. Reakcefkte < containing EcPhoa-sc3D6 protein is deionized by gel filtration.

To demonstrate the efficacy of the EoPhoA-sc3D6 protein, a Western-flotation assay with EIY-1 «test strips (BioRad, USA) was performed. For the control, an analogous test was performed with the acquired antibody, isolated 2Θ-animal cells. As a negative control, the supernatant of all of the E. coli cells was tested and the result of this assay was positive and is shown in FIG. Third

Direct d-α-V-1 antigen using the gpl2Q specific rronoclonal ELISA 25 02, Accesíon δ. 89120601, PELS, Porton Down, UK / byle nano-sena na roicrotizaci plates / stage I, fa. Eune, Denmark / · Layering of culture, containing ují-1 / Dgpsl .S.H.T. Forst mann, P, Henklein and R, von Baehr ψ 1939 · Fine mapping of the immunomodulatory region of the transmemorial of human immunoglobulin virus (HIY-1) by differing peptides and their use in anti-HIY ELISA, J. Virol. Meth. 25,167-173) were coated onto coated microtiter plates. Recombinant gp16C / Barret E.A, Mitterer, W. Muridt, J. Eibl. , M.Eibl, R. C.. Galie, B. Moes, and F. Dorner * 1989 · Iarge-soale production and purification of a recombinant-derived HIY-1 gpl6Q endpoint of its immunogenicity, Aids Hee. and Retroviruasee 1/2 / * 159 * 171 / ·

After washing out the unweighted material, EcPIioA -sc3D6 was dreamed and incubated. The Kevase material was washed again and bound EcPhoA- so3U6 protein was detected by fto-metric pr * i 602 nm with p-nitrophenylphosphate. FIG. 9 is a standard and cut curve of EIV-1 positive culture coatings. '-20-i' · / :: E ~ retit ivr í " ärtir-I! Í ^ I-EII2A i " ·

aňalysis of its irranogen ic i you, Aiďs Bes. and Ruman ix -troviruses 5/2 /: 155-171 / · Then tyly deskr proxnyty IBS +0,1 / Sween 20 + 1 / BSA ·

A solution of 5 µg / µl BcIhoA-sc3B6 phthysis proteinase was 1: 1 with HTV-1 negative / negative! sera and applied to the trawl, pressure control tyl applied with a buffy puir mixed BcIhoA-β316 fusion protein and irrigated. with 60 minutes at 37 cC.loiom the unbound material was recovered, by the addition of p-ritrophenylphosphate, the proportion of the weighed protein was detected. The resultant coloration was photometric at 602 µm. Serum susceptibility was also observed. as a percentage of the serum free amino acid A-sc3B6 protein. Thus, it is shown in FIG. 10, all of which are useful for the ingestible serum binding of the EcPhoA-Sc3B6 fusion protein to gp160. All of the BIV-1 negative sera showed less inhibition than the -17-1 positive serum.

Example 3

Another type of mouse myeloma cell pourity expression was as follows: the β 6 protein in which it was host cell was the 3'-part of the so3 I5 gene was isolated from plasmin pLxsc316 / S2Q IB KO; 3 / partial digestion of λοοäV as well as digestion of the complete HindIII / length fragment: 4µl sp / βp1 with pUC3E6HC '/ i: QQ IB I.I. : 1 / the heavy 3-gene portion of the three-chain and the Hind III was removed. In the remaining vector, a d01 fragment of the β-Jb gene was inserted isolated from agarose gel electrophoresis and purified. The recombined gene consists of a sequence for the leader of the demand for the small antibody of the 3M antibody that is followed by the sequences of the 6c3E6 gene. Plaetnid is designated by 3D6. These constructs allow the sc326 protein to be digested into animal burns. The coding gene was isolated with pse3h6 enzymes liool e SindIII * extending the ends filled with Klenow piiyaza & cloning into E. coli, the expression vector pHoESV is suitable for animal cells suitable for human cells. Another virslnís promoter * & transcriptional termination sequences, such as the fertile hosts of the barefoot growers, are involved in this retrospective measure, leading to the Liboyol structural genes of the molecular environment that allow expression! ger.il to animal cells * In addition, the vector pKoESV has been flying. eelecone marker " reeistenei to nooisyoin " which allows you to * transform * cells in cult?

The so constructed plasmid is denoted by S S S e ee3 6 6 »

This tulle was transferred to the myeloma cells of the Silnie T3KS 3-AgS * 653 / Eearney J.P.A · Eadbruch.B. lieeegnng and Kej © waky, 1979 * A new house myelcsa celi that has lost immunoglobulin express · slon 1: ut permits the conetruction of antibody-secreting hybrid cel lines * J · imrunol · 123 i 1548-1550 / # 2o selekcl transformed A total of 5 clones were selected for antibiotic antibiotic assays to express cloning and correlation, expressing soBB gon «Expression Levels of Individual Clones, tested by an EeISA assay for ancntsin and less than 0.5 and 1 µg, respectively. / ml * culture of transferred myeloma cells and cells containing so3.D6 protoir. was separated by a 5,000 g centrifuge in a test tube, and the excess excess was concentrated 10 times ul. tan * rlGO * out o f f 10000 Ealton * and Milipore / and diafiltrate with 5 th volume »90 kM Tris buffer pH 7 * 2 · > 22- · \ t

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/ j & toysx. J? # '! * ·· · Z $ S7 »ob & λ .olobísg * A praetleal • appxofitfht. val *. . • Λ9 £; ααβ 3 * $ íJj Jxaae · £χ £ ργ £ * W & nhitgxQú BC / * '' 1; ť; 'f, ···.: ·.'. 'l' ·, - 1 l. t. · *, *? *, ^ ·. · *. 1 ·, ·,, * * * \ t cc356 ί * ώϊί.% ”! yyf ístiat ä plaa ^ idtt pXšép ^ G jon-ocx s ® · * '^ trikeríels © r.syi3ái.: a Ineeirtdv ^ », jfta vektoSàs. '.L * K * S · Saísjsea ^ e .fiaft'jO * Fráaô ^'. ·: ¾-l9.ô3V? * EÄuotÍàii oi'terase '* t > «ie iptoicfferôi»; iň'vtn8eot' · eeile '· iafeô'ted Vltk n ^ aatslayJàaa ·, '. r ^ sí ^ eiilan 4eltttti?;: > '^ 1 * .CeH.; δ · 1ο1 ·; '%' $ 1 $ 6 * £ ϊ $ 5 / * Émfo. © kor anta anta o o o o byl byl byl byl sen sen sen sen sen sen sen sen poly poly poly poly poly poly poly poly poly poly poly poly poly poly poly poly poly poly poly poly ult ult ult ult ult ult ult ult ult ult ult ult ult ult ult ult ult ult ult ult ult in Amr.r-'can Type © Culture Collection. 3 to 5 days after transcription of the tulle recombinant virus, microscopically identified and isolated. For the assurance that the isolated reconstitution of the vortices is not contaminated with wild types of vermin, other dietary plaque processes have been added. The infections of the Si9 cells by the recombinant virus lead to lysis of the infected, hune to and to the production of bc3 > 6 proiein in excess lyaate cells after 3-5 days. sc336 protein was purified from this excess and arsysed analogously to that described in Example 3. In this case, it was possible to read the function of this recombinant. protein.

Example 7

Sequences encoding protein avidin / Gope M. L., S.A. Kei-nänon.P.A. Kriste, O.M. Gonr.ealy, tf.G. Beattie,!. Zaruoki-Sohulz, 3, 3/4. 0 # Malley and M, S, Kuloooa, 1937 · FOOLEULAR Clening by the ohiokea avidin c) KA, Kuel. Aoids. fi.es. 1/3 / 13595-36C6 was made by a synthetic oligonucleotide as a synthetic gene such that, additionally, at the end of the 2'-aoliic acid leader / introducer / peptide sequence, the aeical foefatase / Sbuttlewortfc H, J. loraylor and K. Kinton, 1986.3 © -quence of the. gene for alkaline phospbatese Esofcerichia coli JM 33, Bucl. Aôids Bes * 14 / P1 /: 3639 / and at the 3 * - end of the poly linker region for inserts of other genders. The genes inserted into this polylinker region are under appropriate conditions excreted as fusion proteins with the avidin as a fusion partner. -ad er ur; 3 * konoi with these fusions. Proteins are active in the periplasmic prosthetic EschericMe, eoli. This construction unit was inserted into a suitable restriction bowl and a cell expressing vector p1a-3a / Studier I, V, ar. Use of bsoteriophage 17 EKA polyraeraae to direet eelsctlve Mgh-lovel expression cf oloned genee, J. &Amp; ol.Biol «

.V · - ;;; S!

.189:, 113 / c kter which, for the expression of the cloned genes, is a V cer ô ô á g ’7 7 7 ál ál ál or or Ako Ako Ako::::: átor Ako Ako Ako Ako Ako Ako Ako Ako Ako átor. Contains J: Cone Baku. ivector · s.Vn.VI-8n ~ Av, r7- ^ 10: próbtór; · xne.-v't.á - '". , :: ./ '·, -à, · ν " '' '. fi J · i; '. nosti HilA · polyiaerilzy in -v-coli bvm .-. ách ". netrans kribu j s · .- I &.; £ li2tt * 0al e ns or -ust. ^ · Or.oatlá. Culture ',. Λ-; p. '-2 · ·' '' '' '' '' '' '' '' '' '. ... . Ρ. 9 '' -'k '-''- Í, - · · v- ^' - '·:; ; ·· / i * " · '··; '. · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · · E-vj-ae after -' 'fb! I "' " z vekibrBäií'gui 'zicsbv'geňéťic'kôu' 'infor ^ aci;' pro :; ' 27. Here, the infrared, infrared, thus produced 17p plush-to-espresso is also present. clans or psfno in vectors. It is useful for expressing avian and fibrous avidin proteins. ccli very <i51e:;.. its., because uvi - -d in is for ros tone / culture d. coli toxic. The gea was excised from the pUCeepib restriction vector. enzymes and inhaled into polyl in the round of the vector ρΐϊϊ -8a-ΛΥ. the corresponding vector ee denotes p í -3 -3a / vV-sc3D6 · Appropriate E. coli hoetitel cells (e.g., UK5174) were transformed with these cells and cultured. <Jak; a.i! e kulurura - - O # fs, 1 and infected bacteriophage < tb >, < / RTI > and B.á. iiofi'att, 19Gó .Mise öf bacterioph & g 17 HHA polyiaera3e to direct selective high-le-vel expression of ion of geno. J ', Hol. 3 ol. 189: 113 /, which is the gene 1b and * -teriophage? Thus, polynerase 87 results in the expression of the fusion proioin avidium sc Bi in pcriplasraa tic and free from coli. Jataal expression of the proximal rnexima / vein according to the cesium cross-link between 1 and 12 hours after phage infection was. the reconstituted uvol-annoglycyridine protein as described in Example 2, and subjected to ultraf11. The gamma denoentrated solution was purified for Bepha-cryl®, and the solution was concentrated for a second time. The resultant fusion for the avidin with c-21-8 becomes specific. h e c certainty. The column affinity produced was similar to the one in which the analogue of the column was analogous to phi-Iclau. protein, Jjirret et al., (1989), Large-scale Production and Purification of Vaccines and Coronary Diseases of HIVrI gpl1GO and Analysis of its Immunogenic, Aids, Dog. and Human Retrovirueee. · 5/2: 159-171. a. applied to the affinity column and after washing. unbound material; was recombinantly eluted with 3 M rhodanide. .When .toa: ¾¾½ vyťe2kv.T BCU j 'áaalbgické' älédkňm you set the TA " V: bulcé.2. : r and EQ 'vID:? / 0: 1 sequence type by nucleotides and odorating orotein lengths: 1541: p; r

Strand shape: single-strand xepology: circulatory type of molecule: plasmid DKa s insert human cBKa original origin organism: elec tral intestinal introduction: name in the cell 3 DC features: from 1 to bp of the plasmid pUC19 polylinker If " 7. * * VI 1527 n insert ce ~ ~ ~ ~ ~ ~ ~ ~ ~ ~ ~ ~ ~ ~ ~ ~ ~ ~ anti anti ~ ~ anti anti anti anti anti anti anti * vt 1526 " coded region ft 156 1526 " mature pentiá M 15b Vf 533 ”variable region ti 156 ·» «24! 5 ”base structure 1 M i 246 w 2b0 " area 1 specifying the component IV 261 302 " basic symmetric 2 It 302 vt ^ J'2 " region 2 defining the cortex of the mentality • 1 h. K O • r ·: J the basic structure 3 ti T 5 c It 30 · .; M 'obi & st 3 uriujici aonplomentari tu M'. ' 301 vt 63 '} t-clnn c o.mL V * 534 M 152' 6 kongt annn regicnn 1527 »t 15 · 7: · 1α smi d pUC 10 polylinker '···' i .---: · · · · · · · ·. r ··. - · - · ·· in. '** _ t · · ‘. '.w - -':. · - ·· · ·· '·····' '' ''; ·. . ···. * ·. 'f · í ·? ^ Wf; ' -

; Hv '-' Properties of cDHAcapsuleofthefloatconditioningfrom4t-HH ^^ 'SD6 inserto-creamed; to FUCI9. : QTPAATCTCGA ^^ TCQGTACCC GGGGATCCTC TAGAGTCCCA GCCCTGAOAT TCCCAGGTGT 60 -TTCCitCCA ^ GATGÁCKJAČT-GAACACAGAa, GACTCACC · 8 >·; Λ: · - · - -; off "; ATG..GAG TTG G3A CTG AGC TGG: ATT TTC. CTT TTG GCT ATT TTA.AAA- 143 METV-Glu: ^ eu ^ Gly Leu; Ser. He's Phe. Leu; Leu ‘Ala; clay. Leu Lys vV- • · · ·. In " ·· - '-15 -10 - 5 jGGT STC CAG TGT GAA GGGGGGGGGGGGGGGTGGGGCGGGGTGG TTG188

Gly Val Gin Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu

Val Gin Pro Gly Arg Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 15 20 TTC ACC TTT GAT TAT GCC ATG CAC TGG GTC CGG CAA GCT CCA 278

Phe Thr Phe Asn Asp Tyr Ala MET His Trp Val Arg Gin Ala Pro 30 35 GGG AAG GGC: GGG TGG GTC TCA GTA ATA AGG TG GAT AGT 323

Gly Lys Gly Leu Glu Trp Val Ser Gly Ile Ser Trp Asp Ser Ser. 45 50 55 AGT ATA GGC TAT GCG GAC TCT GTG AAG GGC CGA TTC ACC ATC TCC 368 Gain Gly Tyr Asp Asp Val Val Lya Gly Arg Phe Thr White Ser 60 65 70 AGA GACAAflC GCC AAG AAC TCC CTG TAT CTG CAA ATG AAC AGT CTG 413

Arg Asp Asn Ala Lys Asn Ser Leu Tyr Leu Gin MET Asn Ser Leu 75 80 85 AGA GCT GAG GAC AGG GAT 458

Arg Ala Glu Asp MET Ala Leu Tyr Tyr Cys Val Lys Gly Arg Asp 90 95 100

TAC TAT GAT GGT GGT TAT TTC ACG GTT GCT TTT GAT ATC TGG

Tyr Tyr Asp Ser Gly Gly Tyr Phe Thr Val Ala Asp Asp Asp Trp 110 115 120 503 548} · - " iwt-'· · · · W * * rr-'h / S ·' ·. r 's »lv:: v ;;: ··. ·.' ·: ΐ '' · .; i - -; " .. .. - '' -v · * .- · ŕ · -; 'Cc: c ^ ^^ - gcc ϊ -cc -acc;', iAäqsc v -V.: '... v: · :; \ -Ϊ · · Λν &. .z ·: * ·.: - vr · a m * + ·

Val Ser Ser Ale Ser Thr Ly Cly · 125 '' 130: a '· 135.

CCC TGG: TGcJaq; », 140 145 1 G3C ACA OCA GCC CIO OGC TGC CTG GGC AAO GAG TAC TTC CCC GAA 638 01y Thr But Ala Leu Gly Cya Leu Val Lys Asp Tyr Fro Ilu Glu 155 160 165 CCG on ACG OTO TC3 T00 AAC TCA GCC GCC CTO CCCC AGC 33C OTO 663

Fro Val Thr Val Ser Trp Aan Ser Gly AL Leu Thr Ser Gly Val 170 175 130 CAG ACC TTC CCC GTC GTC CTA CAQ TCC TCA

Hie Thr Phe Pro Gin Thr Gin Thr Gin Thr 185 190 195

N AGC AGC OTO.OTO ACC CTG CCC AGC AGC TQQ GGC ACC CAG ACC 773

Ser Ser Val Val Thro Val Serro Ser Ser Leu Gly Thr Gin Thr 200 205 210 * TAC ATG TOC AAC OT AAT CAC AAO CCC AGC AAC AACC OTO GAG 818

Tyr As Cye Asn Vali: Asn His Lys Fro Ser Asn Thr Lys Val Asp 215 220 225 AAAAA GTT OAO CCC AAA TCT TOT GAC AAAAAC CAC ACA TGC CCA 863 i ^ e Lya Val Glu Cye Pro 230? 35 240 CCG TGC CCA CCA GAA CTC CTG GGG GGA CCG TCA GLA CTC 908

For Cys Fro Ala Fro Glu Leu Leu Gly Gly Fro Ser Fhe Leu 245 250 155

Ki 9; ': 3 v: -K. ·: / ·; V: " '/ ..9-23X9; · · / TTtt' CCC ;; .CCA AAAv CCC; AAG: GAC ICC CTC; ATG ATC. TCC CGG ACC. CCT ... S 53 * -Pa-pro Pro 'lys; .pfo ': lys,' Asp Thr, leu KET./Ilé Ser: Af g Thr Pro f: " '260:. ·. · ·; 265 ýr} '. .270 · '”··. · .N' —gag! GTÓj AGA WČ: ct # • in%; - · GTG ^ GTG GAC 'spread & ac ·' '9S8' -n Glu Val Thr, ': Cys.í Val Vaí: Vel Asp: Val Servis Glu' Asp · For Glu 9 'r - ··' ..... Halili wr «· < > -i ·; f 7 5 .r. · -; · '· 23a. ·' * 285, / C ;: AAA and GTC Λ Λ r * A :: U TTC AAC TGG • T · AO - fi v / GTG GAC Cv 0 luu uiiu CTG C AT GCC 1C43 ♦ VgQ lys Phe Aun Trp rrw »* >. Val- Π Π T: G G · · · · · G G G G G G G G 300 300 300 300 300 & & & & & & & & & & & & & & w > GG GAG GAG GAC TAC AAC TCC ACG rG ln X Λ V CGT GTG 10 88 Thys Thr lys Pro 'Arg Glu Glu GIr, Tyr Asn Ser Thr Tyr Arg Val 305 310 315 GTC AGC GTG CTC TGG 'i mn O IKS AAT GGC hu rn Ahu 1133 Val Ser Val leu Thr Val leu Ei with Gin Asp TrpLeu only Gly lys 320 - »/« · r * · 330: GAG TAC AAG TC-C AAG GTC rnrt fi XuG AAC AAA CCC CCA CCA CCC CCC ATC 1173 * Glu Tyr lys Cys lys Valer Asn lys Ala leu For Ala mile 333 340 345 GAG AAA ACC ATC Tce AAA CCC AAA GGG CAG CCC CGA GAA CCA CAG 1223 Ala lys C-Gln Pro Arg Glu Pro Gln. '· - ·. 350 355 360 GTG TAC ACC TAG CCC CCA TCC CGG GAT GAG CTG ACC AAG AAC CAG 1268 Tyr Thr Leu Pro Pro Ser Arg Asp Glu leu Thr lys Asn Gin 365 370 375 GIC AGC CTG . R * 0 X and GTC AAA GGG TTC TAT / A&C WAC AAC 13AC Val A le 13 Thir Cys leu Val lys C-ly Phe Tyr Pro Ser Aop 350 385 330 GCC GTG GAG TGG GAG AGC AAT GGG CAG CGG GAG; AC AC TAC AAG 1358 Ala Val Glu Irp Glu Ser Asn Si Gin Pro Glu Asn Asn Tyr lys 595 4C0 405 1403 Λ. ACC; ACG-CCT CCC. GTG pIG GAC. VC.GAC; GGGC ’TCC Tc Cc Í CTC ECAC Thr! ihr Prà Pro Pro ValAsp lys Sr: AT ^ Trp " ' Gln Gin Gly Ashn Val 425 " Ärg Trp :: 430

Gly 435 5526 1526 01 ac ac a aac: cac. tac aca: ^ THIS? s? ls HIs Glu Ala Leu His Asn Hla IDyr Thr liSl® .....; v.: > .450: CAG AAG AGC TARGET CCGG CCT CCG GGT AAA TGA Gin lys Ser leu Ser Leu Ser Pro Gly lys Stop 455 460

GACCT GCAGG CATGCAAGC2 SEQ ID NO: 2

Sequence type: nucleotides with the corresponding protein dll sequence: 945 party. bases

&Quot; · FuUtQJLA

Strand shape: simple fcroveee ^

Sppology is Circular

Molecule Type: Plasmid-DHA with human cDHA insert Original human organ cellus with immediate experimental origin: Characters: 3D6 from 1 to 21 bp w 22 · 732 · 1 22 27 * n 28 732 - ti 23 · 93 " n 94 " 732 tt 94 " 408 " * 94 ° 162 t tt 163 " 195 w and 196 · 240 " n 241 " 261 " iuatitél, 7¾ žtitŽ-l-í-B-

skull insert insert ka-3D6 5 * untranslated region coding region signal peptide mature peptide variable region baseline 1 region 1 determining complementaxite baseline 2 complementarity determining region 2

Characters .tode 262 áž 357 358 '··· - 373 ^ 75: * 403 409' \ t ÍT32: 733 ".; 905 QC6 ’945 Basic Structure 4

Feature sertovoný do

GTGA .ATIC n «o * * * * * * *. G PAC IC CCACAGC 27 f / T * X X U U AG AG AG AG AG AG AG Gi Gi Gi Gi Gi Gi Gi Gi Gi:::::: 'Xv X · *'. t. V * • v. »·; k > In XV in X «7 GGG V X V f > ry n vxtf CTG / * > Ϊ1Λ V X V 72 Κ2Ϊ Asp - ~ ‘-7 Γ? —R x ίί * ν »W -. ^ Val for Ala C1 rt in? X Γα X e u leu ΟΙ - aiy leu Leu Leu Leu -13 -13 - 3 TGG CTC CCA GGT GCC & About tfilV A ΓΓ-ΛΛ »Al CAG AIG ACC CAG TCT CCT 117 Trp leu for Gly Ala lys Cys Asp ile Gin MET Thr Gin Ser Pro - 3 3 8 TCC ACG CTG TCT. n " u v A-TCT GTA GGA GAG AGA n mn 1jX in ACC A'l'C ACT TGG 162 Ser Thr Leu Ser Ala Ser Val 81y Asp Arg Val Thr i Thr Cs 13 13 23 CGG nnn Jv / υ AGP GAG AGC ATT-AGT AGG TC-G IIG GCC TGG T: AT CAG CAG 207 Arg Ala Ser Gin Ser Al Ser Arg Trp Leu Ala Trp Tyr uln Gin 23. 33 33 AAA CCA CTG ATC ΪΑ2 AAG ΠΟ * UVJi TCT AGT 25 2 Lys Ixo τ ^ ^ ys Pro Pro Pro Pro Pro Pro Pro Pro Pro Pro Pro Pro Pro ye GA GA GA GA GA GA IC * * * * IC IC IC IC IC IC IC. o υϋ ICá A u a r. * V X 1 in AGC n π π • J'jt AGT GGA .ΠΟ rp XV iiGG 297 Uu Gin Ser Gly Val Gly Ser Gly 53 63 63 AGA GAA ítc ni ni rt v > »Xr * v: r. ^ V x in ACC ATC AGC A G G CTG CAG CCT S 'A .T. JÄA GAT ITT 34 2 Ihr Glu Ihe Ihr: eu Thr Ile Ser Ser leu Gin For Asp Asp Phe 73 73 33 '. 32- · · · · · · · - ': i ·, v -:' X ··: - - • 2-ý '>; - * Vr •. . ; · ·. .. · Λ ':; and 'X?; in X '· ¾': " '- in:, - - (' '.'. '. rsfr';,: X '·:' ... 1 '.'. "'-J; ..., • -' · Vx ^ ca; ÄČ.ŠTA: ι ISO ISO '' 'ä ä AG AG AG AG AG AG AG AG AG AG AG AG AG AG AG AG AG T T T T TG T T ^ ^ ^ ^ ^ ^ ^ 7 C73 01c: - G1ä - .. '1! ^ x · .Asn Icr lyr Ser lho 31y Iro - - ÍA X-Gi np ::.: C -'- izil ^ 3 · - · v- Ä &; C P P & & 33 33 33 33 33 33 33 33 33 33 33 33 33 33 33 33 33 33 33 & & & & &&; m -. · - * · "· uuy AČC λ *. *. ťi? .r ΙΛ; CIC '--0¾ A'ICV úťmL · aôš ;: č $ g': ^ cs ·· GC 4 CCA " r ^^ fn Ar ^ J 1 'c-rc 1 · 432 ·,' - l.yo Val ASh 11 «· - 't-hClVlf · Lys-Å * £; Ihr · ··· - r: - Val Ala Ala: l: ro .. .Ser-'Yal o · - ·. ·. * 1C-3 1C3 iiy • i > * n Λ.. * · ATC '; r CCA v ·. ≪:.. * V x x x x x x y x x x y I I I I I I I I I I I I I I I I I I I I I I 32r l lys Aer 32 y uhx Ala 11 rj 123 123 IC i GIT G ;; : .r A - · C ΐ AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC AC Val Val Val Val Val Val Val Val Val Val Val c. G G A GAG ^ C? -3 And i- & GiG G AI Λ J. G G CC CX GAA ICO Οΰϊ A ICC GAG 567 Val Gin. Clfi Cer 31y. t T Gin 2 G G '93 155 G, AG G AG1 CIO Λ C.A GôG r Λ o: < In GAG JtGC A G GAG AGG ACC l.AC AGG CxC 612 Gin Ser Val Ihr 01a O.Λ here A sp.Ser Ivs Aap lor Thx lyr Ser Leu * 163 l & o 17 3 A G C AGG A G C r ·. - · *. GC TAG GAG TAC GAG TAC GAC TAC GC TAC ICC TGC CAA GTC ACC C AT GAG GC C G G GG C GTC GTC 702 A'G G Ty r Ala vyo Glu Vsi Ihr 11h; n, ·: 31 y leu wi-ÍT J ro ·. ≫! 193 c - - 193 2C3 A C A Z ': · G G C 110 Λ C / ·. G G Vri > A J; IU 131 IAG 752 Ihr lys 11: ¾ A lu £ £ £ p p p p p p p!!!!!!!!!!!!!! * - '«, / V' i- .‘i« >

TCAGilCCAG CCIOACCCCC XCCCAXOCTX XAOCCCIATT GCGGTCCTOC AC-Ci'CAXCiIHMlATGCal AAIGIIGOAG GAGAGAG. A. W 352 Al'AAAGIG t ^ f; < > < " .JWJJJ'J / .WW 512 545. in

¾ 3EQ; IiOO: 3 borde: sequence: nucleptides with odespeaking length ·. sequence,: 776 pair d-í px „px q q q q„ „„ „„ „„ px:: ä ä ä ä ä ä ä ä ä ä ä ä ä ä. 72 ií iíií R R? ek ek ek 1 ek ek ek s s s s s rs rs rs rs rs rs rs rs rs rs rs rs rs rs rs rs. with veat & vérsg-a human. ·· pvvoan: r · r · o u organistus: human immediate experimental origin; Cell Threshold 1 Characteristics: 31 b from 1 bp to 13 bp of pHO19 polvlinker TI 14 " 760 «insert sc316 n 14 " 16 tt starting kcdon. 11 14 " 394 tl variable region heavy chain n 17 " 105 The Basic Structure 1 t Ok ého ce 107 107 107 107 107 107 · " 121 TI region 1 of a heavy string specifying coEpleaeritarit t < 122 " 163 tt heavy chain structure 2-C 9 n 164 " 214 tt area 2 of a string chain completing the complication of tt 215 " 310 n the base structure 3 of the n chain ' 311 " 361 n corpusertality determining region 3 of " 352 " 394 tt basic structure 4 toskélao retčzce IT 395 n 440 n lirker w ^ 41 " 760 tt ligand region n 441 " 508 tt lightweight element 1 from. 509 hp to 542. hp light chain region determining the complexity n r- r 0. t! 533 " .company, structure 2 lightweight: / η · Λ / h tézCS:. · '/, .. ·,. hVy-j th. • 339. " ' . 607 si announces. 2 light chain-determining co-complementarity. n r " eoš0v · ': ··': 703 '" '? basic' structure? 3 light; åe-t hce n 7 04 v '7 C · *, " T " ohla s t 5 lightweight e. c s determine Ιοί k o rep 1 e n e n t ar i t u T? 125 " 757 ”base structure 4 of the light chain 75o. 7 oO " stokodon t! 7 61 " 776 " phssnid pUG 19 polylirker

Vlqsinos ^ ju ^ klcn built-in simple string Fv fraintent d

Ka 3D6 inserted into plasmiG rUC11 AAAAGATATTC ccc 13

GG GG GG GG GG GG GG GGG GGG GTA GAG GAG CC T Ket GIu Val Gin leu V Glu Ser Π " J .. Giy Glv leu Val Gin Pro 5 10 15 GGC ». ** * J J J ** \ ** ** ** ** ** ** ** ** ** ** ** ** ** : p-· T * p > ľ G-CA CA CA CA CA CA CA CA CA CA CA CA CA CA CA CA CA CA CA CA CA CA CA CA CA CA λ λ λ λ λ λ λ λ XJiX GCO GGG GGC GGC GGG GAG GCT GCA GGG AG GGC Asn Aop Tyr Ala His Trp Yal Arg Gin Ala Pro Glv K / lys Gly 55 40 45 01G GAG * r n. r · < " T ~. u i'j u. < j hl GG1 f. T. Λ r Γ0 xi 7 i. ΓΓ 'r »r, j-' c / > «, *} ·, 'Vj ÍL j. fc ~ Γ *. Λ v-7 J-3; ^ 7 X ‘rl U X J L X‘ n. le leu Giu Ixp v a.1 Ser Glv íle £ or r Ser Ser Ser Ser Ser ly ly ly ly ly ly ly ly ly ly ly 50 50 50 50 50 50 50 50 50; ', .34. G - G ^ G € G :: G (her: TCà; GTGCAAG / GQC CGA.IIC ACC ATC ICC AGA GAC AAC;

Tyr: Ala Asp Ser Lys Gly Arg Pfce Thr. Ser Arg A sp Asn ;; Λ * 5 vL%. : v. 70; ·. , '. . . 75 .. ^ " GCC - ^^ TCP, " AACAGT CTG AGA GCT GAG

Ala lys. Asn Ser leu Tyr leu GlnCMET Asn Ser leu Arg Ala Glu -. - 80. ' 85 '90

GAC ATG GCC TAT TAC TAC TGT GTA AAA GGC AGA GAT TAT GAT

Asp MET Ala leu Tyr Tyr Cys Val lys Gly Arg Asp Tyr Syr Asp 95 100 105

AGT GGT GGT TAT IIC ACG GII GCT STI GAl A1C TGG GGC CAA GGG

Gly Gly Gly Gly Gly Gly 110 115 120

ACA ATG G1C GTC GGC GGC GGC GGC GGC GGC GGC GGC

Thr MET Val Thr Gly Gly Gly Gly Gly Gly Gly Gly Gly Gly Gly Gly Gly

GGG: GGT GGC GGC GGA GCT GG TCT GAC ATC CAG ATG ACC GAG TCT CCT

Gly Gly Gly Gly Gly Ser Asp Gin MET Thr Gin Ser Pro * 140 145 150

TCC ACC CTG TCT GCA GCT GTA GAC GAC GTC ACC ATC ACT TGC

Ser Thr leu Ser Ala Ser Val Gly Asp Arg Val Ihr Ihr 155 160 165 »

CGG GCC AGI CAG. AGT AGT AGG AGG TTG GCC TGG - CAG CAG

Arg Ala Ser Gin Ser Ile Ser Arg Trp leu Ala Trp Tyr Gin Gin 170 175 180

CCA ACA GTC CAG ACA CCT AAG CTC CTG ATC TAI AAG GCA TCT AGT lys Pro Gly lys Val Pro lys leu leu Tyr lys Ala Ser Ser 185 190 200

TTA GAA AGG GTC GCA TCA GCA TCA GCA GC GG TEC GC GG GC GC GG GC Ser Gly Ser Gly Gly Ser Gly 205 210 £ 15 283 328 373 418 463 508 553 598 643 -35-. : '··. ^ / Α0Α ·: · σίΑ-; ·0 · 10Τ CIC ACC A'ľC AGC AGC CIG-CAG CCI'GGA1; GAI 6 '638

Thx: Glu Phe ihr I, su X h r íle l Sex Sex ls * and Glc Pro Asp A & p 1-he · 220 .v .t ;: Λ v2 £ 5 * 0:; /, 0 ,; -. · - ·; ; /; /. GCA ACT · ACΑ IG · 2AC; IGC A CAA · CAG quotΑΪ ΑΑ.Ϊ- AGP- ϊΑΐ 'ΙΟΐ · ii C G G G G G G G G G G G G G 33 33 33 33 33 33 33 Ala Tlir.:! Yr, lyr .'C y s' Gin Gin, Tyr Asn '; 3er-; 2yr' .Ser.X235-3 --.- 30- ^ 0¾

Phe "Gly Tro V 245

G G G AC: g g; -x

Gly Ihr lys Val Asp Iles lys Arg Stop ---

GCPTCTGCAC CA10TG

Tables substance lycczyn Hlase DlAse IľľA

kor. ε č r. k kc-r-certrace 0.2 ng / nl 15 U /: 1 15 U / ml 100 nE lahulks' 1:. final concentration of decomposition chemicals in cell suspension grade 0b 3 en / nl./ ‘prctein /: 17- / gp160 / rsg / extract-extraction 7C0 lenil 33200 600 100 gt > safaroza 520 ec315 and l'-inner ôhron = to- 1000 372 62 / rraí 130 143 144 24 7 ^

Board-ra. Fig. 2: yields of pure purifiers are purified by inoculating the cellulose-recrystalline microspheres with the tc316 j as the affinity-lip and lip: - e- -36- -36- objsrD / rl / protein / isg / tixr 3500 ....: 7600 1: 2.56. : 350 ^ '5300' 1: 2048 '' 50 72. 1: 10000 stuT en prebytel: kul tury ul-trau .í äà-i 11 r a c e

fO -séfarcza I’sfcul '· p. 3: 3 is a clear purification step for the purification process. 1: the ultra-high-resolution mouse: the mouse mouse.

Claims (6)

-37- . P A T EH ΙΟ V I E. 1 BO. K Y - ^ ^ bi bi bi::::::: aný aný aný aný aný aný aný aný aný aný aný aný aný aný::::: aný aný aný. áhtigéa " EIT-lr in ':: 22 22 že že že že že že že že že že že že že že že že že že že že že že že že lo lo lo lo lo lo lo lo lo lo lo lo lo lo: í -í '' 'w w í í í .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. ..' '' '' The cell line 3, 6. ochézéjíeího 2. A becochinous protein as claimed in claim 1 comprising a variable chain variable region according to SEQ ID NO: 1 * 3 Recombinant protein as claimed. 1 or 2 comprising a light chain organ region according to SEQ ID NO: 2 · 4 4. A recombinant protein according to any one of claims 1 to 3, characterized in that it is subjected to SBQ ID BO: 31 wherein the variable region of the heavy chain variable region of the light chain is linked to p? es linker. 5. A process for the production of a recombinant protein according to claim 1, wherein the DBA transporter of so3D6 or a sequence hybridizing to said insert or sequence derived from the degeneracy of the expressed protein is introduced into a plasmid, with this plasmid, the host is transformed and the construct unit is transformed 6. A method for producing a recombinant protein as claimed in claim 5, characterized in that it is expressed as a fusion protein, in particular with alkaline phosphatase or with avidin. 7. Insertion for use according to claim 5, wherein the insertion of so3D6 has the nucleotide sequence set forth in SEQ ID NO: 3. The purification of the relcombinant protein according to claim 1, wherein the purity of the protein is purified. The specificity of the protein is the specificity of the protein. m / ne ~ -38- v · äiv ·; -.,.. '*' With ri; bilizu; δ-Äp *; soo'podie'n. . On the carrier. Useful for the purification of silicas. A method for purifying or purifying an antigen, characterized in that the isolation or purification is effected by affinity chromatography, optionally using a scobo tein nscoin-sc3S5 -protein as a ligand for the affinity erxo T: at gri. 11 * Multiple addiction of HIV-1 antigen evidence by using a fusion protein containing icphoA-sc3b8. Protein as Bovine Detected and Biliary Protein · 12. A method for the detection of HIV-1 positive sera in a crompable immunoassay using a fusion protein comprising 2cpEoA-sc326 pre-tein as a combined detection and signaling protein.