Purification and properties of two acid phosphatases from midgut glands of abalone Haliotis discus

Hiroshi Yoshida, Hiroshi Sagami, Shigeo Oikawa

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Abstract

Midgut glands of abalone Haliotis discus contained two acid phosphatases [orthophosphoricmonoester phosphohydrolase (acid optimum), EC 3.1.3.2] 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.

Original languageEnglish
Pages (from-to)1447-1454
Number of pages8
JournalJournal of biochemistry
Volume81
Issue number5
Publication statusPublished - 1977 May

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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