| Literature DB >> 1087 |
Abstract
Extracts of acetone-ether powders of bovine thoracic aorta contain lipase activity which has an alkaline pH maximum (7.8-8.4) and is stimulated 4-10-fold by adding serum or isolated apolipoprotein-glutamate to the assay mixture. Serum activation is completely reversed by isolated apolipoprotein-serine or apolipoprotein-alanine. Lipolysis is strongly inhibited by NaCl (0.5 M) and protamine sulfate (1 mg/ml) and partially inhibited by heparin. Based on these characteristics, the lipase is identified as lipoprotein lipase.Entities:
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Year: 1975 PMID: 1087 DOI: 10.1016/0005-2760(75)90031-4
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002