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- W2019231966 abstract "Angiotensin-converting enzyme (EC 3.4.15.1) has been isolated from human liver by chromatofocusing. The isolation procedure permitted us to obtain a 9000-fold purified enzyme with a 22% yield. Specific activity of the angiotensin-converting enzyme was 10 units/mg of protein. The molecular mass of enzyme determined by polyacrylamide gel electrophoresis under denaturing conditions was 150,000. The isoelectric point (4.2–4.3) was also determined by chromatofocusing. The Km values of the enzyme for hippuryl-l-histidyl-l-leucine and N-benzyloxy-carbonyl-l-phenylalanyl-l-histidyl-l-leucine are 5000 and 125 μm, respectively. The human liver angiotensin-converting enzyme is inhibited by bradykinin-potentiating factor SQ 20881 (IC50 = 18 nm)." @default.
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- W2019231966 date "1987-10-01" @default.
- W2019231966 modified "2023-09-27" @default.
- W2019231966 title "Isolation of human liver angiotensin-converting enzyme by chromatofocusing" @default.
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- W2019231966 doi "https://doi.org/10.1016/0003-2697(87)90539-2" @default.
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