Functional characterization of Asp‐317 mutant of human renin expressed in COS cells

FEBS Letters

Hori, Hitoshi¹  Nagahama, Masami¹  Murakami, Kazuo¹  Yamauchi, Takeshi¹ 

[1] Institute of Applied Biochemistry, University of Tsukuba, Ibaraki 305, Japan

关键词: Renin;    Protein engineering;    Optimum pH;    Mutant expression;    (COS cell;    Human);    COS-CM;    COS cells conditioned medium;    AI;    angiotensin I;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    CHO cells;    Chinese hamster ovary cells;   

DOI  :  10.1016/0014-5793(88)80672-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Renin is an unique aspartyl (acid) protease with optimal activity at neutral pH. It has been suggested that Ala-317 of human renin contributes to neutral optimum pH of the enzyme [(1984) FEBS Lett. 174, 102–111]. The hypothesis was verified by the characterization of mutant renin in which Ala-317 was replaced with Asp by a site-directed mutagenesis. Wild-type and mutant renins, which were expressed in COS cells, exhibited different pH-activity profiles and optimum pH of the mutant enzyme was lower than that of the wild-type enzyme. This result suggests that Ala-317 of human renin plays an important role in the determination of optimum pH of the enzyme.

【 授权许可】

Unknown