title: [Identification of Ca(2+)-activated Mg(2+)-dependent ATP-hydrolase activity of membrane microsomal fraction of loach embryo (Misgurnus fossilis L.)].
abstract: The functional confirmation of availability of Ca2+ transport initially-active systems in the embryo cells of loach Misgurnus fossilis L. has been obtained. Using thapsigargin, the specific inhibitor of endoplasmic reticulum of Ca2+, Mg(2+)-ATPase, this enzyme activity was divided into thapsigargin-sensitive (actually endoplasmic reticulum Ca2+, Mg(2+)-ATPase) and thapsigargin-insensitive (plasma membrane Ca2+, Mg(2+)-ATPase) constituents. The Ca(2+)-independent Mg(2+)-dependent ATPase activity makes above 39.7% of the common Ca2+, Mg(2+)-ATPase activity of embryo loach. The periodic changes of Ca2+, Mg(2+)-ATPase activity (except for the changes of plasma membrane Ca2+, Mg(2+)-ATPase activity) were found out, which coincide with periodic [Ca2+]i oscillations during the synchronous divisions of loach blastomers embryos.
authors.forename: M V
authors.initials: MV
authors.lastname: Tselevych
authors.forename: R V
authors.initials: RV
authors.lastname: Fafula
authors.forename: M B
authors.initials: MB
authors.lastname: Halan
authors.forename: D I
authors.initials: DI
authors.lastname: Sanahurs'kyĭ
mesh_terms: D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism; D003531:Cypriniformes / Q000196:embryology / Q000378:metabolism; D004625:Embryo, Nonmammalian / Q000166:cytology / Q000201:enzymology / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000201:enzymology / Q000378:metabolism
chemical_list: D017301:Ca(2+) Mg(2+)-ATPase; D002118:Calcium