Abstract
Summary
Reduced and alkylated γG-globulin from bursectomized and normal chickens had the same elution pattern from Sephadex G-200 columns when either propionic acid or formic acid was used for elution. The phe-nograms obtained from column-separated polypeptide chains were compared, and no difference was found in either the L chain or H chain banding patterns of γG-globulin from bursectomized and normal chickens. These results indicate that the subunit of γG-globulin is the same for bursectomized and normal chickens.
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