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J. Biochem, 1977, Vol. 81, No. 5 1447-1454
© 1977 Japanese Biochemical Society

research-article

Purification and Properties of Two Acid Phosphatases from Midgut Glands of Abalone Haliotis discus

Hiroshi YOSHIDA, Hiroshi SAGAMI1 and Shigeo OIKAWA

Department of Chemistry, Faculty of Science, Tohoku University Sendai, Miyagi 980

Midgut glands of abalone Haliotis discus contained two acid phosphatases [orthophosphoricmonoester phosphohydrolase (acid optimum), EC 3.1.3.2 [EC] ] separable by phosphocellulose column chromatography. They were designated as acid phosphatases I and II in order of elution and were purified 99- and 290-fold, respectively. Purified acid phosphatase II was. nearly homogeneous as judged by polyacrylamide gel electrophoresis. The substrate specificity of acid phosphatase I was narrow, whereas that of acid phosphatase II was broad. Good substrates for acid phosphatase I included p-nitrophenyl phosphate, phosphoenolpyruvate, inorganic pyrophosphate, and nucleoside di- and triphosphates. The acid phosphatases did not require any metal ion for maximum activity and were inhibited by Zn2+, Cu2+, and Hg2+. Fluoride and arsenate were potent inhibitors of both enzymes. The pH optima of acid phosphatases I and II were 5.9 and 5.5, respectively. The molecular weights of acid phosphatases I and II were estimated to be 28,000 and 100,000, respectively, by gel filtration on Sephadex G-l00. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis suggested that acid phosphatase II consists of two identical subunits.

1Present address Chemical Research Institute of Non-aqueous Solutions, Tohoku University, Sendai, Miyagi 980.


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