By N. J. Calvanico, T. B. Tomasi Jr. (auth.), M. Z. Atassi (eds.)
The structural beneficial properties answerable for the immunogenicity of definite components of local protein molecules were of curiosity to immunochem ists and protein chemists for over 3 a long time. despite the fact that, till re cently no concerted attempt used to be (or can be) dedicated to the elucidation of the total 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 distinctive third-dimensional constitution of the protein is critical. Such details used to be now not to be had for a protein until eventually early within the Sixties. This and the truth that protein chemistry used to be no longer in reality sufficiently constructed early within the Nineteen Sixties to let the winning unrav eling of the full antigenic constitution of a protein have been significant purposes for the sluggish development during this box. selection of the antigenic constructions of proteins, as a result, posed a chemical problem of large propor tions. For those purposes, many investigators diverted their cognizance to review of the immunochemistry of amino acid polymers within the wish that the data derived from those structures may turn out beneficial within the realizing of the immunochemistry of proteins. an outstanding many information on those structures have been gathered that experience supplied worthy infor mation at the immune mechanism. regrettably, it has now develop into transparent the data from amino acid polymers has now not helped in less than status the immunochemistry of proteins.
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Additional resources for Immunochemistry of Proteins: Volume 3
Reduction and alkylation had no effect on the C I-fixing ability, indicating that the monomer was equally as 120 6 t:. ~. i~. ~: 40 20 0 JaGl 10'· 10 ' MOlar Concentration of protein incubated with CI ..... Fe &C~2 10'· M Figure 7. y 2 (III) (0), Fab (6), or pFc' (0). Cl activity remaining after preincubation with the test protein is expressed as a percentage of the Cl measured in the absence of the test protein. Reproduced with permission from Yasmeen et al. , Baltimore. , 1976). Painter et al.
Cohen and Becker (1968a,b) have studied the effects of amidination, carbamylation, and benzylation of rabbit antibody on complement fixation. They found that Effector Sites on Antibodies 29 amidination of 54% of the amino groups (lysine) with ethyl acetimidate hydrochloride, or carbamylation of 32% with potassium cyanate, causes a loss of 55% of the complement-fixing ability of the molecule with little effect on antigen binding. At higher levels of conjugation, greater losses occurred caused by nonspecific changes in the molecule, although this was not a result of failure to aggregate since conjugation with these reagents did not affect the association of antibody molecules.
Table IV lists the effector functions and the classes and subclasses they are associated with. It should be mentioned at this point that no definitive function has been found to be associated with the carbohydrate moieties of immunoglobulins, most of which are associated with the Fc fragment. Hinrichs and Smyth (1970) have obtained some evidence that a portion (40%) of rabbit IgG molecules bear a CH 2 oligosaccharide, and these are not transferred across the placental membrane. , close to the inter-Hchain disulfide bond.
Immunochemistry of Proteins: Volume 3 by N. J. Calvanico, T. B. Tomasi Jr. (auth.), M. Z. Atassi (eds.)