title: Behavior of phosphatase isoforms during sclerotium formation in Physarum polycephalum.
abstract: The behavior of phosphatase isoforms under dark-starvation from plasmodium of Physarum polycephalum were investigated to determine their possible roles in sclerotium formation. Two and a half days after dark-starvation, approximately 95% of plasmodia plates formed sclerotia. Specific phosphatase activity increased markedly up to ca. two-fold within the first day of starvation, after which the enzymatic activity decreased rapidly to a level less than the initial level within 2 days of the starvation period. Among the two isoforms of enzyme detected just before sclerotization under dark-starvation conditions, the enzymatic activity of the major isoform (Rm value of 0.6) decreased gradually within 1.5 days of starvation, then linearly to less than 20% of that at the beginning of the observation. Those of other major isoform (Rm value of 0.7) increased up to ca. two-fold within the first day of starvation, then decreased linearly to levels less than that of the first 2 days of the starvation period. Behavior of this isoform strongly suggests that it initiates the formation of sclerotium under dark-starvation conditions.
authors.affiliation: Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University, 2-8-1-Mejirodai, Bunkyo-ku, Tokyo 112-8681, Japan.
authors.forename: Yuhko
authors.initials: Y
authors.lastname: Tanaka
authors.forename: Yohko
authors.initials: Y
authors.lastname: Suzuki
authors.forename: Masako
authors.initials: M
authors.lastname: Osumi
authors.forename: Takako S
authors.initials: TS
authors.lastname: Kaneko
mesh_terms: D000818:Animals; D003624:Darkness; D008027:Light; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D016839:Physarum polycephalum / Q000201:enzymology* / Q000254:growth & development* / Q000648:ultrastructure; D020033:Protein Isoforms / Q000378:metabolism; D013997:Time Factors
chemical_list: D020033:Protein Isoforms; D010744:Phosphoric Monoester Hydrolases