title: Identification of the ATP + Mg-dependent and polycation-stimulated protein phosphatases in the germinal vesicle of the Xenopus oocyte.
abstract: Two protein phosphatase activities were characterized in the germinal vesicle of Xenopus laevis oocytes after manual dissection of the nucleus. One enzyme can be classified as an active form of the ATP + Mg-dependent (AMD) phosphatase, the other as a polycation-stimulated (PCS) phosphatase. The activity of the PCS phosphatase is localized exclusively in the soluble compartment of the nucleus (nucleoplasm). The catalytic subunit of the AMD phosphatase activity is associated either with the nuclear particulate fraction or with an inhibitory subunit in the nucleoplasm.
authors.affiliation: Laboratoire de Physiologie de la Reproduction, Université Pierre et Marie Curie, Paris, France.
authors.forename: C
authors.initials: C
authors.lastname: Jessus
authors.forename: J
authors.initials: J
authors.lastname: Goris
authors.forename: S
authors.initials: S
authors.lastname: Staquet
authors.forename: X
authors.initials: X
authors.lastname: Cayla
authors.forename: R
authors.initials: R
authors.lastname: Ozon
authors.forename: W
authors.initials: W
authors.lastname: Merlevede
mesh_terms: D000818:Animals; D002412:Cations; D002467:Cell Nucleus / Q000201:enzymology; D009865:Oocytes / Q000201:enzymology* / Q000648:ultrastructure; D010749:Phosphoprotein Phosphatases / Q000302:isolation & purification*; D011073:Polyamines; D000071228:Polyelectrolytes; D011108:Polymers; D014982:Xenopus laevis
chemical_list: D002412:Cations; D010749:Phosphoprotein Phosphatases; D011073:Polyamines; D000071228:Polyelectrolytes; D011108:Polymers