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  • Title: Hormone-sensitive lipase from bovine adipose tissue.
    Author: Cordle SR, Colbran RJ, Yeaman SJ.
    Journal: Biochim Biophys Acta; 1986 Jun 16; 887(1):51-7. PubMed ID: 3708011.
    Abstract:
    Hormone-sensitive lipase has been purified to near homogeneity from bovine perirenal adipose tissue. The purification method involves isoelectric precipitation at pH 5.0, followed by partial solubilisation in Triton N-101 and ion-exchange chromatography on DE-52. After additional solubilisation, the enzyme is further purified by chromatography on phenyl-Sepharose and heparin-Sepharose. This procedure can be completed within three working days and yields approx. 30 units of enzyme with a specific activity of 30 U/mg. The enzyme has been identified as a polypeptide of Mr 84 000 by affinity labelling with [3H]diisopropyl fluorophosphate. This polypeptide comprises approx. 60-80% of the protein in the final preparation, as judged by scanning densitometry of SDS-polyacrylamide gels stained with silver or with Coomassie blue R. The polypeptide of Mr 84 000 serves as a substrate for cyclic AMP-dependent protein kinase, phosphorylation correlating with activation of the lipase. Polyclonal antibody to the lipase has been raised in a rabbit and shown to specifically cross-react with the Mr 84 000 subunit.
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