By Jaroslava Turková (Eds.)

Bioaffinity chromatography is now the popular selection for the purification, selection or elimination of many biologically energetic ingredients. this article comprises info on biologically energetic ingredients with their affinants, stable helps and techniques of coupling, summarized in tables overlaying classical, high-performance liquid and large-scale bioaffinity chromatography. Optimization of the practise and using hugely lively and good biospecific adsorbents is mentioned in numerous chapters. Following a bankruptcy facing the alternative of affinity ligands, affinity-sorbent bonding is defined intimately. different chapters supply details on sturdy helps, the most typical coupling methods and a basic dialogue of sorption and elution. a number of functions of bioaffinity chromatography are defined, reminiscent of quantitative assessment of biospecific complexes and lots of makes use of in drugs and within the biotechnology undefined.

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The isolated monospecific antibody in a subsequent step, was again coupled to the solid carrier, and a column was prepared for the sorption of the antigen on a large scale. 22 SMALL AMOUNT OF ANTIGEN CRWE ANTIGEN PUMPED THRaKin COLUMN AND TOPRERRE AN IMMWLIZED ANTIGEN COLUMN LARGE WNTITIES OF CRUDE ANTIGEN Fig. 4. Cyclic bioaffinity chromatography by bootstrapping technique. , Anal. ,68 (1975) 371-393. Fig. 5 shows a scheme for the fully automatic preparation of monospecific antibodies and antigens (Eveleigh, 1982).

J. H. , Pierce Chem. , Rockford, Illinois, 1983, pp. 521-530. The affinity constants of the biospecific complexes of modified pepstatin were determined by Kay and coworkers (1982). The value of the affmity constant Ki of the complex of cathepsin D with isovalerylpepstatin was equal to 10'' M-' . e. a drop of three orders of magnitude. 1. Hydrogen-bonding involving P3P2Pi and P'i residues I h w t r t i n I r r w n t Ptnicillorpsin Ut1 MI ....... t W 1 7 0" Utl e0 ....... '.. Ut1 M Ua1 eo .......

1979). The bond between the lectin and the aldehyde group of the solid support was stabilized by reduction using sodium borohydride. Carboxypeptidase Y was liberated from the 37 A 8 . I O.! O! 0 E F ! : z 0: a a m ! 0 8 ca LlO20304050 FRACTION NUMBER Fig. 3. 3. 01 M phosphate buffer (pH 7). 1 M sodium acetate (pH 6). 0). 5). Data from J. , J. , 376 (1986) 315-321. - complex with immobilized concanavalin A by borate buffer. In Chapter 4 we shall discuss the advantages of oriented immobilizationof glycoproteinsthrough their carbohydrate moieties.

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