By N. J. Calvanico, T. B. Tomasi Jr. (auth.), M. Z. Atassi (eds.)

The structural beneficial properties chargeable for the immunogenicity of definite elements of local protein molecules were of curiosity to immunochem­ ists and protein chemists for over 3 a long time. in spite of the fact that, until eventually re­ cently no concerted attempt was once (or will be) dedicated to the elucidation of the full antigenic constitution of a protein. to ensure that those en­ deavors to achieve success and significant, wisdom of either the amino acid series and the unique three-d constitution of the protein is critical. Such details was once no longer on hand for a protein until eventually early within the Sixties. This and the truth that protein chemistry was once no longer in reality sufficiently constructed early within the Sixties to let the profitable unrav­ eling of the complete antigenic constitution of a protein have been significant purposes for the gradual growth during this box. decision of the antigenic constructions of proteins, consequently, posed a chemical problem of huge propor­ tions. For those purposes, many investigators diverted their realization to check of the immunochemistry of amino acid polymers within the wish that the knowledge derived from those platforms may turn out worthy within the realizing of the immunochemistry of proteins. an outstanding many info on those platforms have been accrued that experience supplied beneficial infor­ mation at the immune mechanism. regrettably, it has now develop into transparent the knowledge from amino acid polymers has now not helped in less than­ status the immunochemistry of proteins.

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This stability is even more remarkable in view of the lack of disulfide bonds. The significance of protein A binding to immunoglobulins is not clear. Protein A is present in the cell walls of most (90%) strains of S. aureus but absent in S. , 1971). 9%) present in coagulase-positive (pathogenic) S. , 1971) and absent from coagulase-negative strains (largely nonpathogens). , 1969). , 1970b), but the protein is also found extracellularly (Forsgren, 1969). For these reasons protein A is thought to be a factor contributing to the pathogenicity of the organisms possessing it.

The native protein is the principal reactor, and aggregation is not required. This finding was not supported by the work of Augener et al. (1971), who showed that all IgM proteins examined, including four of the putative non-complement-fixing group supplied by MacKenzie, interacted with highly purified Clq as assessed by analytical ultracentrifugation. 0 and recovered in a low molecular weight peptide fraction released from the Fc fragment. Moreover, the peptide recombined with the (FchI-', restoring the C I-fixing capacity.

MOpe 173 Val Eu Ser GIn Mope 173 Lys Thr Ala GIn Leu Arg Eu Pro Ser Asp Asp 270 Ile Mope 173 Eu MOPC 173 Eu 260 :" ... Q a ~. = Q. Dl :I Q ~. , 1976). In both cases the fragments appear to be random coils. , 1977). In addition, treatment of CH 3 with pepsin results in a fragment which fixes Cl (K. J. Dorrington, personal communication). It therefore appears that while the physiological site for Cl fixation is probably on the CH 2 domain, other sites may also fix Cl, probably nonspecifically, although a physiological role for these sites under certain conditions has not been excluded.

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