Characterization of multiple molecular forms of Mg2+-dependent protein phosphatase from Saccharomyces cerevisiae1

Takashi Murakami, Takayasu Kobayashi, Takayuki Terasawa, Motoko Ohnishi, Shunsuke Kato, Yoji Sasahara, Masaaki Itoh, Takeshi Nakano, Shinri Tamura

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5 Citations (Scopus)


Three molecular species of Mg2+-dependent protein phosphatase (MPPs-1, -2, and -3) were isolated by DEAE cellulose column chromatography and gel filtration from an extract of Saccharomyces cerevisiae. MPP-1 was further purified 150-fold by chromatography using thio-phosphorylated myosin light chain-agarose. MPPs-1, -2, and -3 were distinct from the major acid and alkaline phosphatases, and their activities were not affected by okadaic acid, microcystin-LR or Ca2+, and calmodulin, resembling the enzymatic properties of type 2C protein phosphatase of mammalian cells. The apparent molecular masses of MPPs-1, -2, and -3 on gel filtration were 53, 112, and 128 kDa, respectively. It was demonstrated that MPP-1 is a globular protein of 53-55 kDa and that MPPs-2 and -3 are oligomeric proteins that dissociate upon sucrose density gradient centrifugation, generating catalytic proteins of about 50 kDa. Since the substrate specificities of MPPs-1, -2, and -3 differed from each other both before and after sucrose density gradient centrifugation, it was suggested that the catalytic proteins of these three enzymes are distinct molecular species.

Original languageEnglish
Pages (from-to)762-766
Number of pages5
JournalJournal of Biochemistry
Issue number4
Publication statusPublished - 1994 Apr


  • Okadaic acid
  • Oligomeric enzyme
  • Protein phosphatase
  • Yeast


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