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

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.