Modification of the substrate specificity of rat hepatic lipase by collagenase treatment

Abstract

Collagenase is currently used in the isolation of rat hepatocytes, but it rapidly inactivates the heparin-releasable triacylglycerol lipase of the liver. Since collagenase-isolated liver cells contain a heparin-releasable monoacylglycerol hydrolase, a study was made on the effect of collagenase treatment on the substrate specificity of purified heparin-releasable lipase of rat liver. Incubation of the purified lipase with collagenase selectively decreased the triacylglycerol lipase activity of the enzyme with no effect on the monoacylglycerol hydrolase activity. Gel filtration of the lipase before and after collagenase treatment indicated cleavage of a small molecular weight fragment from the enzyme. This resulted in a preparation with less triacylglycerol lipase activity but still capable of monoacylglycerol hydrolysis.