New PDF release: The Antigens. Volume VI

By Michael Sela

ISBN-10: 0126355061

ISBN-13: 9780126355062

The Antigens, quantity VI is a complete treatise masking all facets of antigens, together with their chemistry and biology in addition to their immunologic position and expression. Parasite antigens and their immunogenicity in contaminated hosts are explored, besides the character of the antibody-combining web site and the phenomenon of immunological tolerance.

Comprised of 3 chapters, this quantity starts off with a dialogue at the dynamic elements of the functionality of antibodies, paying specific cognizance to the constitution of immunoglobulins and the folding in their domain names; the dynamics of segmental flexibility; the kinetics of antibody-hapten organization and the kinetic expression of uncomplicated interplay; and the conformational transitions in the antibody molecule caused by way of hapten binding. the subsequent bankruptcy makes a speciality of the immunogenicity of parasite antigens in contaminated hosts, mentioning such parasites as trypanosomes, Schistosoma mansoni, and Fasciola hepatica. The final bankruptcy offers with immunological tolerance, its induction and length, and its impact at the specificity of the immune response.

This monograph might be of curiosity to practitioners and researchers in immunology, experimental and scientific medication, biochemistry, and different disciplines.

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The latter, relatively slow rates observed for the association between Fd' and L are markedly slower than the rates reported by Friedman et al. (1978) for a homogeneous human L and H chain recombination (6 x 106 M _ 1 sec - 1 ). Whether this difference in rates reflects differences in the proteins used or in experimental conditions is not clarified. The systematic and extensive investigation of the reassociation be­ tween H and L chains by Pre val and Fougereau (1976) has shown that out of 40 distinct combinations of chains derived from 12 human mye­ lomas, 80% occurred between autologous ones.

The reason why faster rotational re­ laxation modes due to the putative motion at the elbow have not been resolved by the anisotropy decay kinetics of probes like the DNS hap- 26 Israel Pecht ten is still unclear. Preliminary data obtained by studying the aniso­ tropy decay of tryptophans in different Ig fragments (I. Pecht and L. Stryer, unpublished, 1978; Pecht, 1980) give reason to believe that such motions could indeed be resolved, with relaxation times in the range of 1 0 - 2 0 nsec. Significantly, monitoring the spin label attached covalently to IgG and its fragments, Timofeev et al (1978) reached similar conclusions concerning flexibility at the Fc domains.

It is significant to note that from this structural analysis other features of flexibility have also emerged. Thus, in addition to variability in the spatial arrangement of the Fab arms relative to their Fc which is afforded by the hinge re­ gion, there are other flexible points. T h e relative arrangement of the V and C domains in the Fab arms were found to be different among the different molecules whose Fab structure has been determined. , 1978; cf. Section II). , 1978). The extent of flexibility at the V - C switch is probably expressed in a more extreme form when considering the profoundly different con­ formations that have b e e n found for light chain dimers.

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The Antigens. Volume VI by Michael Sela

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