Abstract
Crude lipoprotein lipase, extracted from rat adipose tissue or heart acetone-ether powders, was purified about 300 and 350 fold respectively by affinity chromatography. Artifactual increments in the density of very low density lipoprotein, noted after incubation with the crude lipoprotein lipase extract from adipose tissue, were abolished when the purified enzyme was used. Purified enzymes from both tissues showed similar modifications of activity in the presence of activators and inhibitors. The triglyceride moieties of various natural substrates were preferentially hydrolysed in the order Very low density lipoprotein > Serum chylomicrons > Thoracic duct chylomicrons by both enzymes.
| Original language | English |
|---|---|
| Pages (from-to) | 808-814 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 57 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Apr 8 1974 |
| Externally published | Yes |
Bibliographical note
Funding Information:ACKNOWLEDGEMENTS: The authors thank assistance. Dr. P.J. Dolphin is a Canadian supported by grants from the Medical Research Foundation.
ASJC Scopus Subject Areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology