Antibodies: Their structure and function by M.W. Steward

By M.W. Steward

The pupil of organic technology in his ultimate years as an undergraduate and his first years as a graduate is predicted to achieve a few familiarity with present examine on the frontiers of his self-discipline. New study paintings is released in a puzzling variety of courses and is unavoidably con­ cerned with the trivialities of the topic. The sheer variety of learn journals and papers additionally motives confusion and problems of assimilation. overview articles often presuppose a history wisdom of the sphere and are necessarily fairly limited in scope. there's therefore a necessity for brief yet authoritative introductions to these parts of recent organic learn that are both no longer handled in usual introductory textbooks or will not be handled in enough element to allow the scholar to head on from them to learn scholarly stories with revenue. This sequence of books is designed to fulfill this desire. The authors were requested to provide a quick define in their topic assuming that their readers can have learn and remembered a lot of a customary introductory textbook of biology. This define then units out to supply through construction in this foundation, the conceptual framework during which glossy study paintings is progressing and goals to offer the reader a sign of the issues, either conceptual and functional, which needs to be conquer if growth is to be maintained.

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Antibodies: Their structure and function

The coed of organic technology in his ultimate years as an undergraduate and his first years as a graduate is anticipated to achieve a few familiarity with present examine on the frontiers of his self-discipline. New examine paintings is released in a puzzling range of courses and is necessarily con­ cerned with the trivia of the topic.

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Extra resources for Antibodies: Their structure and function

Example text

The radioactivity inside the antibody compartment represents bound and free hapten and that outside represents free hapten. Thus by subtraction, the amount of bound hapten is obtained. This process is repeated for several hapten concentrations using the same antibody concentration. The affinity of the antibody may then be calculated from the data by the methods described above. (b) Ammonium sulphate precipitation In this technique, the insolubility of antibody and hence antibody-hapten complexes in 50% saturated ammonium sulphate is used [21].

G. with anti-protein antibodies. 3 below). The following is a brief outline of the derivation of equations frequently used for affmity calculations using the data from such experiments. Detailed derivations can be obtained from references [11] and [12]. 2) 1 + K[Ag] where r = moles hapten bound per mole of antibody present, [A bAg] = bound antibody concentration, (Ab) free antibody concentration, [Ag] free hapten concentration, n =antibody valence,K =equilibrium constant. Thus a plot of r/[Ag] versus r (Scatchard plot) for a range of antigen concentrations allows n, the antibody valence and K to be obtained (Fig.

Wissler, F. C. and Lipman, L. N. (1960), Science, 132, 1770. [3] Edelman, G. M. and Poulite, M. D. (1961),1. Exp. , 113,861. [4] Porter, R. R. (1962), in Basic Problems of Neoplastic Disease, Columbia University Press, New York. [5] Porter, R. R. 81. [6] Valentine, R. C. and Green, N. M. (1967),1. , 27, 615. [7] Cathou, R. E. (1979), in Immunoglobulins (eds G. W. Litman and R. A. Good), Plenum, New York, p. 37. [8] Putnam, R. , Wikler, M. and Shinoda, T. (1967), Cold Spring Harbor Symposium on Quantitative Biology, 32, 9.

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