Relation between Gm(f) and the Structure of the γ-Globulin Molecule

Abstract

THE serologically detectable genetically determined antigens Gm(a) and Gm(b) are restricted to the Fc (fast) fragment of the A (Heavy) polypeptide chains of human gammaG-globulin1. In contrast, Gm(bw) is present in the Fab, (slow) fragment, and its serological activity seems to depend on the ‘quaternary’ structure of the intact gammaG-molecule2. Gm(f) activity also is localized to the Fab fragment of gammaG-globulin3,4, and is also present in the 5S product obtained by pepsin digestion of the 7S gammaG-molecule4 (Table 1); Gm(a) and Gm(b) activities are lost during pepsin digestion. Recent studies5 indicate that Gm(f) and Gm(bw) are similar but not identical. We report here the results of experiments with anti-Gm(f) and isolated A and B chains of gammaG-globulin.

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GOLD, E., MANDY, W. & FUDENBERG, H. Relation between Gm(f) and the Structure of the γ-Globulin Molecule. Nature 207, 1099–1101 (1965). https://doi.org/10.1038/2071099a0

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