The Antibody Molecule by Alfred Nisonoff

By Alfred Nisonoff

The Antibody Molecule experiences the literature resulting in present wisdom of the constitution of immunoglobulins. The e-book starts by way of outlining many of the uncomplicated structural features of immunoglobulins with no bringing up the references on which the knowledge is predicated. Separate chapters stick with masking the chemical nature of the energetic web site of an antibody molecule and mechanisms of interplay with hapten; the overall structural positive aspects and homes of a number of the periods of human immunoglobulin; and amino acid sequences of human and mouse L chains and of human and rabbit H chains. next chapters care for the evolution of the immunoglobulin periods; particular houses of mouse, guinea pig, rabbit, and horse immunoglobulins; idiotypic specificities of immunglobulins; and the genetic keep an eye on of antibodies.
This ebook is intended for immunologists who've now not individually saw the advance of this interesting interval within the historical past of immunology. it is going to additionally offer precious supplemental interpreting for the intense pupil or investigator who needs to get to grips with the character of the antibody molecule, its genetic keep watch over, and mode of motion.

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A more detailed investigation of antibodies specific for poly-L-alanyl determinants was reported by Schechter (23), who utilized specifically purified rabbit antibodies directed to polyalanyl side chains. He found that the trimer was actually as effective as the tetramer, provided that the terminal carboxylate group of the trimer was amidated O II (—C—NH2). II. Specificity to Synthetic Polypeptides 35 It was concluded that the negative charge of the terminal carboxylate group is disadvantageous to binding; in the case of the trimer this can be overcome either by amidation or by adding a fourth alanyl group, either of which reacts with the carboxylate of the third alanyl group.

Anti-Dnp antibodies are of particular interest because the Dnp group, when attached to protein, is uncharged; many of the earlier studies of specificity had involved antibodies to charged hapten groups. Antibodies of very high affinity (A^0 ^ 108 M"1) can be elicited by prolonged immunization with Dnp-protein conjugates (14). These antibody populations are highly heterogeneous, showing a broad spectrum of combining affinities. 3. The results were obtained by measurements of fluorescence quenching (Section VI,D) or, in the case of one hapten of low affinity, by equilibrium dialysis using radiolabeled hapten.

Size of the Combining Region of Antibodies to a-Dnp-Polylysine Schlossman and Levine (30) prepared antibodies in guinea pigs against poly-L-lysine to which Dnp (2,4-dinitrophenyl) groups were coupled at the α-amino position: NO2 0 2 N—ά ))—NH—Lys—Lys—Lys---Lys —Lys—Lys—COOH To prepare such antibodies, an α-Dnp-substituted polymer, which had an average chain length of 11 lysine groups, was conjugated to bovine serum albumin for use as the immunogen. Synthetic poly-L-lysine preparations of increasing length, with Dnp groups attached at the a-NH2-terminal position, were tested as inhibitors of the precipitin reaction of the immunogen with its rabbit antibodies.

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