| Autor: |
Cook, Kenneth G., Yeaman, Stephen J., Strålfors, Peter, Fredrikson, Gudrun, Belfrage, Per |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 6/15/82, Vol. 125 Issue 1, p245-249, 5p, 3 Charts |
| Abstrakt: |
Several properties of the cytosolic cholesterol ester hydrolase from bovine adrenal cortex were investigated and those properties were compared directly with those of the well-characterised hormone-sensitive lipase, the rate-limiting enzyme in adipose tissue lipolysis. Properties examined included: (a) activity against different substrates; (b) susceptibility to inhibition by NaF, Hg2+ ions and diisopropyl fluorophosphonate: (c) subunit molecular weight as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate: (d) ability to serve as a substrate for cyclic AMP-dependent protein kinase; (e) effect of phosphorylation on enzyme activity; and (f) degradation pattern of polypeptides following limited proteolysis. In all respects the two enzymes exhibited essentially identical characteristics. It is therefore concluded that the same protein, or two very similar proteins, catalyses the hydrolysis of cholesterol esters in adrenal cortex and lipolysis in adipose tissue. The implication of this finding is discussed in relation to the hormonal control of steroidogenesis in adrenal cortex and of lipolysis in adipose tissue. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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