MODIFICATION OF THE SUBSTRATE-SPECIFICITY OF RAT HEPATIC LIPASE BY COLLAGENASE TREATMENT
- 1 January 1979
- journal article
- research article
- Vol. 57 (3) , 192-195
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 MW fragment from the enzyme. This resulted in a preparation with less triacylglycerol lipase activity but still capable of monoacylglycerol hydrolysis.This publication has 6 references indexed in Scilit:
- A comparison of the lipolytic activities in liver perfusates and liver plasma membranes from ratsBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1978
- Complete loss of heparin-releasable triacylglycerol lipase activity after collagenase treatment of the rat liverBiochemical Journal, 1978
- Monoacylglycerol accumulation in low and high density lipoproteins during the hydrolysis of very low density lipoprotein triacylglycerol by lipoprotein lipaseBiochemical and Biophysical Research Communications, 1978
- Determination of protein in adipose tissue extractsJournal of Lipid Research, 1976
- Rat high density lipoprotein subfraction (HDL3) uptake and catabolism by isolated rat liver parenchymal cells.Journal of Biological Chemistry, 1976
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951