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Glycosylation of Ovine Prolactin during Cell-Free Biosynthesis^*

THOMAS W. STRICKLAND and JOHN G. PIERCE

Department of Biological Chemistry, UCLA School of Medicine Los Angeles, Calfornia 90024

Abstract

Recently, a glycosylated form of ovine PRL (oPRL) was isolated from a crude pituitary preparation. As glycosylation of PRL was unexpected and because the composition of the oligosaccharide-containing peptide indicated the carbohydrate portion to be extensively degraded, studies of the glycosylation of oPRL during cell-free biosynthesis were initiated. Two glycosylated forms of oPRL can be recognized when biosynthesis occurs in ovine pituitary microsomes. Both forms are converted to mature PRL by digestion with endoglycosidase H and, thus, appear to contain only asparagine-linked, high mannose-type carbohydrate moieties. In contrast, immunoprecipitates from bovine pituitary microsomes consist of the expected (and nonglycosylated) pre-PRL and PRL. The results are consistent with the absence of a sequence segment in the bovine hormone which permits glycosylation (Asn-X-Ser- or Thr-) and the presence of the segment Asn3l-Leu-Ser- in the ovine hormone. The occurrence of two glycosylated forms of oPRL is not understood; it may result from an additional site in oPRL capable of glycosylation. (Endocrinology 116: 1295-1298, 1985)

Footnotes

^* This work was supported in part by USPHS Grant AM-18005. A summary of this work was presented at The Seventh International Congress of Endocrinology, Quebec City, Canada, July 1984.

To whom requests for reprints should be addressed.

Received September 25, 1984.

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