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J. Biochem, 1976, Vol. 80, No. 2 389-396
© 1976 Japanese Biochemical Society

research-article

Purification and Properties of Oxytocinase (Cystine Amino-peptidase) from Monkey Placenta1

Motoharu HAYASHI and Kiyoshi OSHIMA

Department of Physiology, Primate Research Institute, Kyoto University Inuyama, Aichi 484

Oxytocinase (cystyl-aminopeptidase) [EC 3.4.11.3 [EC] ] was isolated from monkey placenta in a purified form by a six-step procedure comprising extraction from monkey placenta homogenate, ammonium sulfate fractionation, repeated chromatography on hydroxylapatite, chromatography on a column of DEAE-cellulose and gel filtration on a column of Sephadex G-200. The purified enzyme showed a single band on polyacrylamide disc electrophoresis. Oxytocin was inactivated by this enzyme preparation. The enzyme hydrolyzed several aminoacyl-ß-naphthylamides. A terminal amino group was required for enzyme activity. The molecular weight of the purified enzyme was estimated to be 87, 000 by gel filtration and 83,000 by sodium dodecyl sulfate gel electrophoresis. Other properties of the enzyme, the effects of metal ions and various chemical reagents on the enzyme activity, the pH optimum, and Km values for a number of aminoacyl-ß-naphthylamides were also examined.

1 This study was supported by a grant from the Ministry of Education, Science and Culture, of Japan.


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