Phospholipase C purification and specificity with respect to individual phospholipids and brain microsomal membrane phospholipids |
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| Authors: | W L Stahl |
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| Institution: | 1. Neurochemistry Laboratory, Veterans Administration Hospital Seattle, Washington 98195 U.S.A.;2. The Departements of Physiology and Biophysics and Medicine (Neurology), University of Washington School of Medicine, Seattle, Washington 98195 U.S.A. |
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| Abstract: | Phospholipase C was purified from a crude preparation derived from Cl. perfringens utilizing a one-step polypreparative electrophoresis procedure. The purified enzyme has a molecular weight of 46,500 ± 500 and is essentially free of proteolytic and phospholipase A enzymatic activities. It exhibited the following substrate specificity: PC ≥ SM > PS > PI, lyso PC. PE was hydrolyzed when PC was present.Treatment of brain microsomes with purified phospholipase C reduced membrane phospholipids by 69%. All phospholipids were attacked including PE. PC was reduced to 4% and all other phospholipids to 23–43% of their control levels. Total fatty acid composition of brain microsomes was not affected by phospholipase C action. |
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| Keywords: | Reprint requests to: Neurochemistry Laboratory Veterans Administration Hospital 4435 Beacon Avenue South Seattle WA 98108 |
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