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Monoacylglycerol lipase activity in cardiac myocytes
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Monoacylglycerol lipase activity in homogenates of isolated myocardial cells (myocytes) from rat hearts was recovered in both particulate and soluble subcellular fractions. The activity present in the microsomal (100 000 × g pellet) fraction was solubilized by treatment with Triton X-100 and combined with the 100 000 × g supernatant fraction; the properties of monoacylglycerol lipase were investigated with this soluble enzyme preparation. The Km for the hydrolysis of a 2-monoolein substrate was 16 μM. The rates of hydrolysis of 1-monoolein and 2-monoolein were identical, and 1-monoolein was a competitive inhibitor (Ki = 20 μM) of the hydrolysis of 2-monoolein. Monoacylglycerol lipase activity was regulated by product inhibition according to the following order of potency: fatty acyl CoA > free fatty acids > fatty acyl carnitine.
Canadian Science Publishing
Title: Monoacylglycerol lipase activity in cardiac myocytes
Description:
Monoacylglycerol lipase activity in homogenates of isolated myocardial cells (myocytes) from rat hearts was recovered in both particulate and soluble subcellular fractions.
The activity present in the microsomal (100 000 × g pellet) fraction was solubilized by treatment with Triton X-100 and combined with the 100 000 × g supernatant fraction; the properties of monoacylglycerol lipase were investigated with this soluble enzyme preparation.
The Km for the hydrolysis of a 2-monoolein substrate was 16 μM.
The rates of hydrolysis of 1-monoolein and 2-monoolein were identical, and 1-monoolein was a competitive inhibitor (Ki = 20 μM) of the hydrolysis of 2-monoolein.
Monoacylglycerol lipase activity was regulated by product inhibition according to the following order of potency: fatty acyl CoA > free fatty acids > fatty acyl carnitine.
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