Microsomal Ca2+- and phospholipid-dependent protein kinase. Identification and in vitro binding studies.
A Ca2+- and phospholipid-dependent protein kinase (CaPK) has been identified in rat liver microsomes. CaPK isolated from liver cytosol bound to smooth microsomes in the presence of 100 microM CaCl2. A saturation in binding was observed when a 5-fold excess of enzyme over that present in microsomes had become bound. The microsomal CaPK and 50% of the enzyme bound in vitro was not removed by EGTA treatment. This suggests that Ca2+ is required for the binding of CaPK to microsomes, but not for the retention of the enzyme on the membrane.
D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D002118:Calcium / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D066298:In Vitro Techniques; D008862:Microsomes, Liver / Q000201:enzymology*; D010743:Phospholipids / Q000494:pharmacology*; D011485:Protein Binding; D011493:Protein Kinase C; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats
D010743:Phospholipids; D011494:Protein Kinases; D011493:Protein Kinase C; D002118:Calcium