Abstract
1.1. Optimal assay conditions were determined for a triacylglycerol lipase purified from human post-heparin plasma. The characteristics of this enzyme were compared to those of crude post-heparin plasma and adipose tissue lipoprotein lipase activities.2.2. Assay in solutions of high ionic strength (i.e. l M NaCl) resulted in activation of the purified enzyme. This activation was shown to be associated with a marked reduction in apparent molecular weight by gel filtration experiments.3.3. A pH optimum of 9.0 was observed for the purified triacylglycerol lipase. Evidence is presented for the existence of a factor in pre-heparin plasma which can cause a shift in the pH optimum to 7.6.4.4. The characteristics of the crude post-heparin plasma triacylglycerol lipase activity are compatible with the presence of both this enzyme and a lipase with the properties of adipose tissue lipoprotein lipase.
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