CHROMATOGRAPHIC ANALYSIS OF HUMAN SEMINAL ANGIOTENSIN I CONVERTING ENZYME ISOFORMS

Document Type : Original Article

Authors

1 *Department of Biochemistry, Science University of Tokyo Graduate School, Shinjuku-ku 158 Tokyo, Japan

2 Pharmacology Department, Faculty of Veterinary Medicine, Zagazig University, University, Egypt

Abstract

Separation of isoforms of angiotensin I converting enzyme (EC 3.4.15.1, ACE) from human semen was attempted by chromatographic procedures. The crude ACE was fractionated on DEAE-Sephadex A-25 and Sephadex G-200 columns. Two ACE components were separated out in the first DEAE-SEphadex A-25 chromatography. The two ACE preparations (S-I and S-II) were separately applied to gel filtration through a Sephadex G-200 column. S-I was further separated into two peaks. Elution of the first peak showed MW about 150KD, while the second peak corresponded to MW about 100KD. S-II was eluted as a single Peak at an elution position corresponding to MW about 150 KD. At least three ACE components were separated out from the seminal extract.

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