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The Journal of Immunology, 1963, 91: 448-459.
Copyright © 1963 by The American Association of Immunologists, Inc.

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Structural Basis for the Differences between Type I and Type II Human {gamma}-Globulin Molecules

John L. Fahey

From the Metabolism Service, National Cancer Institute, National Institutes of Health, Bethesda 14, Maryland

Abstract

Polypeptide chains common to all {gamma}-globulin groups (i.e., 6.6 S {gamma}-globulins, beta2A-globulins, {gamma}1-macroglobulins, and {gamma}-microglobulins) were found in two forms (I and II) differing in antigenic composition. The two types of common polypeptides were characterized as "L" chains with a molecular weight of about 20,000.

Each 160,000 molecular weight human {gamma}-globulin molecule appears to be composed of two "L" polypeptide chains with identical (type I or II) antigenic properties (which account for 25% of the molecule) and class specific ({gamma}, beta2A or {gamma}1M-type) "H" components (which account for the remaining 75% of the molecule).




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