Polypeptide Chains of Rabbit Gamma Globulin

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Abstract
Rabbit gamma globulin has been extensively reduced, and its polypeptide chains separated by gel filtration on Sephadex G-200 in 5 M Edge-notched cards in an inverted system of indexing may be used satisfactorily to analyze research data which concern a small series of individuals but a large number of highly variable characteristics in a short-term research project.guanidine hydrochloride. The larger H (or A) chains make up two-thirds of the molecule and have a molecular weight of approximately 55,000 each. The smaller L (or B) chains account for the other one-third and have a molecular weight of approximately 25,000 each. The data are consistent with a model of the gamma globulin molecule that has two H and two L chains.

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