Angiotension I Converting Enzymes in Rat Epididymis

概要

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When the homogenate of rat epididymis was fractionated by centrifugation, 55% of the total activity of angiotensin I converting enzyme (EC 3.4.15.1; ACE) was found in the 100000×g supernatant (soluble fraction) and about 40% in the 100000×g pellet (particulate fraction).ACE from the soluble fraction was eluted as a single peak in TEAE-cellulose chromatography. This ACE was found to have smaller molecular size than rat testicular ACE by gel filtration through a Sephadex G-200 column.On the other hand, in the case of ACE solubilized from the particulate fraction by treatment with sodium deoxycholate, two peaks of the activity (P-I and P-II fractions) were detected in TEAE-cellulose chromatography. ACE from the P-I fraction was found to have a smaller molecular size than rat testicular ACE, while ACE from the P-II fraction was found to have the same molecular size as rat pulmonary ACE when they were analyzed by gel filtration through the same column as mentioned above.Thus, in the present investigation, different form of ACE were detected in rat epididymis. This is the first report of the presence of ACEs with molecular sizes smaller than that of rat testicular ACE (which had been reported to have lower molecular weight than rat pulmonary ACE) in soluble and particle fractions of rat epididymis.
公益社団法人日本薬学会の論文
1986-01-25