Phospholipase C activity in plasma membranes isolated from lapine synovial cells in monolayer culture |
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| Authors: | R J Rothenberg R W Moskowitz C J Malemud |
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| Institution: | 1. The Cartilage Research Laboratory, Department of Medicine, Case Western Reserve University, Cleveland, Ohio 44106 USA;2. Department of Developmental Genetics and Anatomy, Case Western Reserve University, Cleveland, Ohio 44106 USA |
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| Abstract: | Two phosphorylase kinase activities were resolved by DEAE-cellulose chromatography. The main activity peak was enriched 2800-fold, the minor appeared to be an aggregate of the enzyme. Phosphorylase kinase also phosphorylated histone and casein with no changes in phosphorylation ratios throughout the preparation steps but was most active on yeast phosphorylase. The molecular weight was 29000 +/- 2000. ATP, UTP, GTP served as substrates while CTP was inactive. Mg-ions activated the kinase without inhibition at high concentrations (30 mM). In addition to this cAMP-independent kinase, cAMP-dependent protein kinase also phosphorylated phosphorylase. The catalytic subunit and phosphorylase kinase were not identical since the latter was not inhibited by yeast cAMP binding protein. |
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| Keywords: | arachidonic acid BSS balanced salt solution PI phosphatidylinositol PS phosphatidylserine PC phosphatidylcholine PE phosphatidylethanolamine G-6-PD glucose-6 phosphate dehydrogenase |
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