Protein phosphatase 2A from Xenopus oocytes
- 16 December 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 295 (1-3) , 185-188
- https://doi.org/10.1016/0014-5793(91)81414-4
Abstract
A polyclonal antibody was raised against bacterially produced catalytic α subunit of protein phosphatase 2A (PP2AC) cloned from Xenopus ovarian library. The amount of PP2AC in Xenopus oocytes determined by Western blot analysis was 1 ng/μg of cytosolic protein. The antibody depleted PP2AC from oocyte extracts in association with 6 components (40, 62, 65, 80, 85 and 90 kDa). Prophase- and metaphase-arrested oocytes contained identical amounts of PP2AC. Metaphase oocytes showed one specific change in the 62 kDa protein associated with PP2ACKeywords
This publication has 24 references indexed in Scilit:
- Protein phosphatases are involved in the in vivo activation of histone H1 kinase in mouse oocyteDevelopmental Biology, 1990
- In vivo progesterone regulation of protein phosphatase activity in Xenopus oocytesDevelopmental Biology, 1990
- Universal control mechanism regulating onset of M-phaseNature, 1990
- Characterization of MPF activation by okadaic acid in Xenopus oocyteCell Differentiation and Development, 1990
- Involvement of protein phosphatases 1 and 2A in the control of M phase-promoting factor activity in starfish.The Journal of cell biology, 1989
- Purification of a p47 phosphoprotein from Xenopus laevis oocytes and identification as an in vivo and in vitro p34cdc2 substrateFEBS Letters, 1989
- Okadaic acid, a specific protein phosphatase inhibitor, induces maturation and MPF formation in Xenopus laevis oocytesFEBS Letters, 1989
- A possible role for Mg2+ ions in the induction of meiotic maturation of Xenopus oocyteCell Differentiation, 1986
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970