By Thomas J. Kindt, J. Donald Capra (auth.)

The Antibody Enigma is a a little bit own view of the antibody variety query from investigators who've spent the previous 18 years attempting to penetrate the enigma. it's not and was once no longer intended to be an all-embracing comprehensively referenced evaluate of the topic of antibody range. as a result of the subjective standpoint, there are un­ doubtedly omissions of knowledge that others deliberate to be seminal, and if we have now indignant an individual by way of omitting their very own contribution we sin­ cerelyapologize. we now have lived with "The Enigma" off and on for the earlier years. it's been either exertions and reliable enjoyable yet, exceptionally, it's been a studying adventure. there have been a number of tough judgements to make in placing jointly the ultimate textual content, yet probably the main tricky was once de­ ciding upon a preventing element. the sphere of antibody range is almost immediately having fun with an extraordinary enlargement of data, and due to this it was once very tempting to look forward to additional advancements in hopes of tying up as many unfastened ends as attainable. This used to be made up our minds opposed to for numerous purposes; the key issue used to be that the undertaking used to be becoming burdensome for either one of us. From a extra target perspective this seems to be an inexpensive time to forestall our exposition.

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3. Exceptions to the Correlation of Idiotypy and Binding Site Although the majority of evidence suggested that there was a direct relationship between antibody-combining site and the idiotypic determinants, some disturbing exceptions were noted. Kelus and Gell (1967) 44 CHAPTER 2 in their studies of antiproteus antibodies observed that anti-Id antibodies would react with the antibody even when it was combined with the bacterium. Carson and Weigert (1973) noted that certain idiotypes were not ligand-modifiable and therefore represented determinants in portions of the V region other than the antibody-binding site.

For example, if a group of V regions all bear the same marker, then they must be identical to the extent required by this shared marker but must be sufficiently different from one another to account for their different antigenic specificities. 2. A schematic of rabbit IgG showing the locations on the molecule of the major allotypic groups. The numbers in parentheses indicate the major alleles for each group. A number of additional alleles for the group b allotypes have recently been described. The IgG molecules may have lambda rather than kappa chains; these express the group c allotypes (c7, c21).

In retrospect, this was a fortuitous circumstance that allowed a rapid initial burst of information on this subject. At the time these serologic studies were begun, techniques for protein structure determination were not sufficiently developed to handle large complex molecules, nor were there available procedures for protein isolation suitable for the mixtures of molecules contained in most antibody populations. Indeed, the concept that a single molecule might have multiple, disulfide-linked subunits was years away.

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