1. A comparative study of post-heparin lipolytic activity and a purified human plasma triacylglycerol lipase
- Author
-
Heiner Greten, W. Virgil Brown, and Christian Ehnholm
- Subjects
Time Factors ,Size-exclusion chromatography ,Biophysics ,Triacylglycerol lipase ,Adipose tissue ,Sodium Chloride ,Post-heparin lipolytic activity ,Biochemistry ,Dogs ,Endocrinology ,Animals ,Humans ,Tromethamine ,Lipase ,Triglycerides ,chemistry.chemical_classification ,Lipoprotein lipase ,Chromatography ,biology ,Heparin ,Chemistry ,Lipid Mobilization ,Osmolar Concentration ,Hydrogen-Ion Concentration ,Chromatography, Ion Exchange ,Enzyme Activation ,Kinetics ,Lipoprotein Lipase ,Enzyme ,Adipose Tissue ,Liver ,Organ Specificity ,Ionic strength ,Chromatography, Gel ,biology.protein - 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.
- Published
- 1974