Modification of fibrinogen chains during synthesis: glycosylation of B.beta. and .gamma. chains

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Abstract
Specific immunoprecipitation and affinity chromatography on Con [concanavalin] A-Sepharose of in vitro translated products derived from rat liver mRNA, total polysomes and rough microsomes were used to determine temporal events of glycosylation of the subunits of fibrinogen. The A.alpha. chain is not glycosylated; both the b.beta. and the .gamma. chains have carbohydrate clusters (probably Asn linked). The .gamma. chain receives its core carbohydrate as an early cotranslational event. The B.beta. chain is glycosylated later and is probably glycosylated at the time of polypeptide termination or shortly after it is released from the ribosome into the cisternal space of the rough endoplasmic reticulum.

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