Purification and characterization of membrane-bound phospholipase C specific for phosphoinositides from human platelets.
Y Banno, Y Yada, Y Nozawa - Journal of Biological Chemistry, 1988 - ASBMB
Two peaks (mPLC-I and mPLC-II) of phosphatidylinositol 4, 5-bisphosphate (PIP2)-
hydrolyzing activity were resolved when 1% sodium cholate extract from particulate fractions
of human platelet was chromatographed on a heparin-Sepharose column. The major peak
of enzyme activity (mPLC-II) was purified to homogeneity by a combination of Fast Q-
Sepharose, heparin-Sepharose, Ultrogel AcA-44, Mono Q, Superose 6-12 combination
column, and Superose 12 column chromatographies. The specific activity increased 2,700 …
hydrolyzing activity were resolved when 1% sodium cholate extract from particulate fractions
of human platelet was chromatographed on a heparin-Sepharose column. The major peak
of enzyme activity (mPLC-II) was purified to homogeneity by a combination of Fast Q-
Sepharose, heparin-Sepharose, Ultrogel AcA-44, Mono Q, Superose 6-12 combination
column, and Superose 12 column chromatographies. The specific activity increased 2,700 …