Abstract
The isolation of hydrolysis products from glyceryl [1- 14C]trioleate provided a sensitive and reproducible assay system to measure plasma post-heparin lipolytic activity and adipose tissue lipoprotein lipase (glycerol-ester hydrolase, EC 3.1.1.3). Essentially no lipolytic activity was detected in pre-heparin plasma. With this system hydrolysis at 37° ceased by 60 min and temperatures lower than 30° were required for linear hydrolysis rates. At 27° zero-order kinetics could be obtained for more than 2 h. Hydrolysis of triglyceride by adipose tissue lipoprotein lipase was also greater at 27° than at 37°. Up to 50% of the original post-heparin lipolytic activity was retained after lyophilization and extraction of plasma with organic solvents, permitting measurement of enzyme activity after nearly complete removal of endogenous substrate, even in patients with gross hypertriglyceridemia. These studies thus suggest two ways that assay of post-heparin lipolytic activity may be improved: the use of lower temperatures to achieve greater stability of the enzymatic activity and delipidation of post-heparin plasma to remove competition from endogenous glycerides.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
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