Cormier P, Osborne H B, Bassez T, Poulhe R, Bellé R, Mulner-Lorillon O
Laboratoire de Physiologie de la Reproduction, INRA, URA CNRS 1449, Université Pierre et Marie Curie, Paris, France.
FEBS Lett. 1991 Dec 16;295(1-3):185-8. doi: 10.1016/0014-5793(91)81414-4.
A polyclonal antibody was raised against bacterially produced catalytic alpha 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/microgram 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 PP2AC.