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 K_m of mutant angiotensinogen was 3 times increased, but the V_max was not affected by the mutation.