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Abstract
Chicken γ-globulin has been purified and subjected to physical-chemical and to enzymatic degradation studies. The normal γ-globulins have a molecular weight near 206,000, have an isoelectric point near 5·2, and contain near 3·1 per cent hexose. Electrophoretic “fast” and “slow” components are produced with both papain and pepsin. The papain fast components retain some antigen combining activity. It is suggested that the normal chicken γ-globulins are more similar to the γA- than to the γG-globulins of mammalian species.
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