Biochemistry of Antibodies by Roal’d S. Nezlin (auth.)

By Roal’d S. Nezlin (auth.)

When the historical past of immunology within the 20th century is written, the last decade of the 1960's will, possibly, stand out because the interval of maximum boost within the improvement of molecular immunology. it really is applicable and invaluable, consequently, schol­ arly and built-in presentation of this growth will be made to be had in English. the interpretation of Dr. Nezlin's "Biochem­ istry of Antibodies" from Russian admirably fulfills this want within the kind of a systematic monograph directed to clinical and biolog­ ical scientists. the looks of this monograph additionally serves to stress the conceptual unification of numerous immunological phenomena which has emerged from development in molecular immunology. This cohesion is a final result of the main function performed by way of the antibody mol­ ecule (either in resolution or cell-bound) in each organic strategy thoroughly defined as immunological. certainly, immunology as an self sufficient normal technology could be defined because the research of the constitution, interactions, and biosynthes is of the antibody molecule.

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Use of acids is more efficient since dissociation of the specific complex takes place at pH values at which antibody damage is negligible. 3,86% splits off [105]. 4 [133]. 7 [136]. Acid treatment of antibody at these pH values has almost no effect on their capacity to react with antigen. 5. As a result of acid treatment at pH 2 for 24 hr at 0°, the precipitating capacity of antibody was reduced by 3%. It should be mentioned that acids, nevertheless, cause changes in the molecular structure of antibodies which affect their aggregation capacity.

It is important that this binding can take place at temperatures and pH values at which proteins are not denatured and retain their capacity to react with specific antibodies. Compounds containing acid chloride or isocyanate groups are able to react with proteins. In several instances, these groups have been used to attach proteins to insoluble supports [16,46,87]. ) [71, 154, 156]. In [155), carboxymethylcellulose was used as the insoluble support, and dicyclohexylcarbodiimide was used for binding, which presumably took place via an amide bond between the antibody amino group and the carboxyl group of carboxymethylcellulose: Cellulose -0 -CH2 -CO -OH + RNH2 Cellulose-0-CH2 -CO-NH -R +H 20.

Gurvich, "Use of antibodies linked to antigen on an insoluble support for specific extraction of various proteins: Biokhimiya 29(6):1054 (1964). L. A. Zil'ber, Foundations of Immunology [in Russian], Medgiz, Moscow (1959). L. A. Zil'ber and G. I. Abelev, Virology and Immunology of Cancer [in Russian], Medgiz, Moscow (1962). E. A. Zotikov, R. M. Urinson, and L. P. Poreshina, "Sensitive method for detection of weak antibodies," Patol. Fiziol. i Eksperim. Terapiya 7(4):71 (1963). A. P. Konikov, "Modification of the complement fixation reaction for quantitative determination of antigens and antibodies," Zh.

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