Unusual phosphatase activity resistant to SDS and pronase treatments in Xenopus ovary.
An unusual phosphatase, which is resistant to treatment by 5% SDS and proteolytic enzymes, was isolated as two types, 1 and 2, from pronase-treated homogenates of Xenopus ovary. The molecular sizes of types 1 and 2 were estimated as about 140 kDa and more than 2 x 10(4) kDa, respectively, by gel filtration, but as 140 and 130 kDa as a catalytic unit, respectively, by electrophoresis, implying that whereas type 1 might be composed of catalytic unit alone, type 2 is a multicomponent complex consisting of a 130-kDa catalytic unit. Both activities were sensitive to nucleases but resistant to tested proteolytic enzymes. These findings suggest that the unusual phosphatase activity is attributable to a polynucleotide.
Sugimoto
T
T
Department of Biology and Geosciences, Faculty of Science, Shizuoka University, Ohya 836, Shizuoka, 422-8529, Japan.
Amano
M
M
Tokumoto
T
T
Ishikawa
K
K
D000818:Animals; D004789:Enzyme Activation; D004795:Enzyme Stability; D005260:Female; D010053:Ovary / Q000201:enzymology*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D011402:Pronase; D012967:Sodium Dodecyl Sulfate; D014981:Xenopus
D012967:Sodium Dodecyl Sulfate; D010749:Phosphoprotein Phosphatases; D011402:Pronase