Partial purification and characterization of two forms of phosphatidylinositol 4-phosphate 5-kinase from human platelet membrane.
The phosphatidylinositol 4-phosphate 5-kinase (PIP kinase) was isolated from the cholate extract of human platelet membranes. Two major activity peaks (PIP kinase I and PIP kinase II) were resolved by successive chromatographies on Fast Q-Sepharose, heparin-Sepharose, Mono Q and heparin-agarose columns. The PIP kinase I appears to be distinct from the PIP kinase II with regard to Mr (51 kDa and 47 kDa as determined by SDS-PAGE). The two forms of PIP kinase showed similarity in Km for ATP and Mg2+ dependency, but some differences were observed in effects of Mn2+ and phosphatidylethanolamine on the activity.
Suzuki
T
T
Department of Biochemistry, Gifu University School of Medicine, Japan.
Banno
Y
Y
Nozawa
Y
Y
D001792:Blood Platelets / Q000201:enzymology* / Q000648:ultrastructure; D002462:Cell Membrane / Q000201:enzymology; D006801:Humans; D006868:Hydrolysis; D007527:Isoenzymes / Q000097:blood* / Q000302:isolation & purification; D008970:Molecular Weight; D010770:Phosphotransferases / Q000097:blood* / Q000302:isolation & purification; D017853:Phosphotransferases (Alcohol Group Acceptor); D010738:Type C Phospholipases / Q000378:metabolism
D007527:Isoenzymes; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C020077:1-phosphatidylinositol-4-phosphate 5-kinase; D010738:Type C Phospholipases