Dipeptidyl carboxypeptidase from human seminal plasma

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 330 000. The pI in isoelectric focusing was 4.6--5.0 and the optimum pH 7.7--8.0. The enzyme is activated by c...

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Bibliographic Details
Published inBiochimica et biophysica acta Vol. 523; no. 2; pp. 469 - 476
Main Authors Depierre, D, Bargetzi, J P, Roth, M
Format Journal Article
LanguageEnglish
Published Netherlands 12.04.1978
Subjects
Dipeptides
Humans
Kinetics
Male
Molecular Weight
Peptidyl-Dipeptidase A - metabolism
Semen - enzymology
Substrate Specificity
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Summary: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 330 000. The pI 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 greater than bradykinin greater than Bz-Gly-Gly-Gly greater than Boc-Phe-Ala-Pro greater than Bz-Gly-His-Leu greater than angiotensin I.
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ISSN:0006-3002
DOI:10.1016/0005-2744(78)90049-9