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Role of N ‐linked oligosaccharides attached to human renin expressed in COS cells
Author(s) -
Hori Hitoshi,
Yoshino Teruhiko,
Ishizuka Yasuyuki,
Yamauchi Takeshi,
Murakami Kazuo
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80777-4
Subject(s) - asparagine , glycosylation , mutant , biochemistry , site directed mutagenesis , mutagenesis , alanine , chemistry , n linked glycosylation , residue (chemistry) , amino acid residue , amino acid , biology , peptide sequence , glycoprotein , gene , glycan
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‐S 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 wildtype 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.