Effects of glycosylation of the residue at position 14 in ovine angiotensinogen on the human renin reaction.
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.
Inui
Y
Y
United Graduate School of Agricultural Science, Gifu University, Japan.
Orihashi
T
T
Nakagawa
T
T
Ebihara
A
A
Suzuki
F
F
Nakamura
Y
Y
D000595:Amino Acid Sequence; D000808:Angiotensinogen / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000818:Animals; D001216:Asparagine / Q000737:chemistry; D001483:Base Sequence; D015153:Blotting, Western; D016466:CHO Cells; D002851:Chromatography, High Pressure Liquid; D006224:Cricetinae; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D012083:Renin / Q000032:analysis / Q000378:metabolism*; D017421:Sequence Analysis; D012694:Serine / Q000737:chemistry; D012756:Sheep
D000808:Angiotensinogen; D012694:Serine; D001216:Asparagine; D012083:Renin