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- W2076459089 abstract "Dipeptidyl carboxypeptidase (angiotensin I converting enzyme) was purified from human seminal plasma. The apparent relative molecular mass determined by gel filtration on Sephadex G-200 was 330 0000. The ptI in isoelectric focusing was 4.6–5.0 and the optimum pH 7.7–8.0. The enzyme is activated by chloride. These properties are similar to those reported for the lung enzyme. The specificity is that of a carboxypeptidase releasing dipeptides. A study of different substrates showed the activity to be highest with Z-Leu-Gly-Gly, followed by Z-Phe-His-Leu > bradykinin > Bz-Gly-Gly-Gly > Boc-Phe-Ala-Pro > Bz-Gly-His-Leu > angiotensin I." @default.
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- W2076459089 date "1978-04-01" @default.
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- W2076459089 title "Dipeptidyl carboxypeptidase from human seminal plasma" @default.
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- W2076459089 doi "https://doi.org/10.1016/0005-2744(78)90049-9" @default.
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