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• W2034140275 abstract "<h2>Abstract</h2> Cardiac sarcolemma was isolated from hamster and dog and was examined for phospholipase A activity using 1-acyl [2-¹⁴C]-linoleoyl3-glycerophosphorylethanolamine as substrate. Hamster sarcolemmal preparations contained phospholipases A₁ which had optimal activity at pH 6.0 and pH 9.0 in the presence of 5 mm Ca²⁺; EDTA was a potent inhibitor of phospholipase activity at both pHs. The specific activities of the hamster sarcolemmal phospholipases A₁ were increased 5.9-fold (pH 6.0) and 8.4-fold (pH 9.0) over the homogenate, while the increase in specific activity of the sarcolemmal marker enzyme, ouabain-sensitive (Na⁺-K⁺)-Mg⁺-ATPase, was 7.5-fold; thus both the (Na⁺+K⁺)-Mg⁺-ATPase and phospholipase A₁ activities were associated with enriched cardiac sarcolemmal membranes. Canine myocardial sarcolemmal preparations also contained a phospholipase A that had optimal activity at pH 7.0 in the presence of 5 mm Ca²⁺ and the enzyme exhibited apparent specificity for the 2-position. The phospholipase A and (Na⁺+K⁺)-Mg²⁺-ATPase activities were similarly enriched in the canine sarcolemmal preparation. These endogenous, calcium-stimulated phospholipase A activities may be important constituents of the myocardial sarcolemmal membrane; they may modulate the lipid environment of the sarcolemma and may regulate the activity of lipid-dependent enzymes as well as alter membrane permeability." @default.
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• W2034140275 date "1978-10-01" @default.
• W2034140275 modified "2023-09-27" @default.
• W2034140275 title "Phospholipase A activity of highly enriched preparations of cardiac sarcolemma from hamster and dog" @default.
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• W2034140275 doi "https://doi.org/10.1016/0022-2828(78)90338-3" @default.
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