Purification of protein phosphatase from hen oviduct.
Two protein phosphatases of 103 and 29 kDa as determined by gel filtration, were purified from hen oviducts. The 103 -kDa phosphatase was purified 7300-fold to near homogeneity and dissociated into two polypeptides in the presence of SDS. Molecular masses of these polypeptides were estimated to be 60 and 38 kDa by SDS-polyacrylamide slab gel electrophoresis using the buffer system of Laemmli, but 68 and 35 kDa using the buffer system of Weber and Osborn. The stoichiometry of these polypeptides was approx 1:1 according to the densitometric analysis of gels at 550 nm. The 29 -kDa phosphatase was purified 2900-fold. Both phosphatases dephosphorylated the alpha-subunit of phosphorylase kinase more rapidly than the beta-subunit.
Kanayama
K
K
Wada
K
K
Negami
A
A
Yamamura
H
H
Tanabe
T
T
D000818:Animals; D002645:Chickens; D005260:Female; D008970:Molecular Weight; D010057:Oviducts / Q000201:enzymology*; D010749:Phosphoprotein Phosphatases / Q000302:isolation & purification*
D010749:Phosphoprotein Phosphatases