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Effects of glycosylation of the residue at position 14 in ovine angiotensinogen on the human renin reaction.

作者信息

Inui Y, Orihashi T, Nakagawa T, Ebihara A, Suzuki F, Nakamura Y

机构信息

United Graduate School of Agricultural Science, Gifu University, Japan.

出版信息

Biosci Biotechnol Biochem. 1998 Aug;62(8):1612-4. doi: 10.1271/bbb.62.1612.

DOI:10.1271/bbb.62.1612
PMID:9757569
Abstract

A mutant angiotensinogen, S14N, in which Ser14 of ovine angiotensinogen was replaced by Asn to form a N-glycosylation site, was produced in CHO cells. The molecular weight was about 3,000 larger than that of wild-type ovine angiotensinogen, indicating that S14N angiotensinogen was glycosylated at Asn14. In the reaction with human renin, the km of mutant angiotensinogen was 3 times increased, but the Vmax was not affected by the mutation.

摘要

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