Purification of polymeric phospholipase Cs from human platelets.
Two types of cytosolic phospholipase C specific for phosphoinositides were purified from human platelets. The molecular masses of the purified enzymes were 440 and 290 kDa. These enzymes were concluded to be respectively a trimer and a dimer of homologous 146 kDa polypeptides. The 146 kDa polypeptide may be an immunologically novel isozyme among the 140-150 kDa PLC isozymes. Both enzymes hydrolyzed phosphatidylinositol and phosphatidylinositol 4,5-bisphosphate in a Ca2(+)-dependent manner.
Moriyama
T
T
Research Institute for Food Science, Kyoto University.
Narita
H
H
Oki
M
M
Matsuura
T
T
Kito
M
M
D001792:Blood Platelets / Q000187:drug effects / Q000201:enzymology*; D002118:Calcium / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification*; D008970:Molecular Weight; D019269:Phosphatidylinositol 4,5-Diphosphate; D010716:Phosphatidylinositols / Q000378:metabolism; D012680:Sensitivity and Specificity; D013379:Substrate Specificity; D010738:Type C Phospholipases / Q000737:chemistry / Q000302:isolation & purification*
D007527:Isoenzymes; D019269:Phosphatidylinositol 4,5-Diphosphate; D010716:Phosphatidylinositols; D010738:Type C Phospholipases; D002118:Calcium