Hori H, Yoshino T, Ishizuka Y, Yamauchi T, Murakami K
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
FEBS Lett. 1988 May 23;232(2):391-4. doi: 10.1016/0014-5793(88)80777-4.
One or both of two putative N-glycosylation sites (at asparagine-5 and -75) of human renin was eliminated by amino acid replacement of the asparagine residue with an alanine residue using site-directed mutagenesis. The three glycosylation-deficient renins (Asn-5, Asn-75, Asn-5 and -75 mutants) were expressed in COS cells and secreted into the conditioned media. The secreted amounts of the three mutants were different from one another, although the mutant and wild-type renins had practically the same specific activity. An Asn-5 and -75 mutant which did not contain any glycosylation sites was unstable in the medium, suggesting that the N-linked oligosaccharides play an important role in stabilization of human renin.
