Udupa, Padmanabha EG (2012) Purification and characterization of ram epididymal angiotensin converting enzyme. Journal of Medical Science & Technology, 1 (2). pp. 32-42. ISSN 1694-1217

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Abstract

Angiotensin converting enzyme (ACE) from ram epididymis was purified to homogeneity. The purification procedure consists of ion exchange chromatography on DEAE Sephadex A-50, gel filtration on Sephacryl S-300 and biogel hydroxyl apatite chromatography. The purified ACE showed single band on native PAGE, reducing SDS-PAGE and non reducing SDS-PAGE. The molecular mass of purified ACE was determined as 102 k Da by SDS-PAGE. The Km ,Vmax, Kcat and Kcat / Km values of purified epididymal ACE were 1.9mM, 10μ moles/min/mg , 29420 min-1 and 15.48 x 106 M -1 min‾1 for Hip-His- Leu respectively. Arginyl, glutamyl , tyrosyl and Iysyl groups are functional residues of epididymal ACE. EDTA and 1,10-phenanthroline completely inhibited epididymal ACE activity at 57μ M concentration. In presence of cobalt epididymal ACE activity increased to two folds.

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