Glycosylation at position 14 of ovine angiotensinogen increases its Km for human renin by 3-fold without affecting Vmax.
Glycosylation effects on ovine angiotensinogen kinetics warrant caution before human extrapolation; leaves open its role in clinical renin-angiotensin regulation.
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.
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INUI et al. (1998) studied this question.
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