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Hydrolysis of tri- and monoacylglycerol by lipoprotein lipase: evidence for a common active site

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Author

Summary, in English

The relationship between triacylglycerol and monoacylglycerol hydrolyzing activities of purified rat heart lipoprotein lipase was studied using emulsified trioleoylglycerol and micellar or albumin-bound monooleoylglycerol as substrates. The maximal reaction rates obtained with the two substrates were similar (650 and 550 nmol of fatty acid released per min per mg of protein, respectively). Addition of apolipoprotein C-II or serum increased the maximal reaction rate for the trioleolyglycerol hydrolyzing activity about four-fold, but had no effect on the monooleolyglycerol hydrolyzing activity. Hydolysis of the two substrates apparently takes place at the same active site of the enzyme since (1) mutual competitive inhibition between the substrates could be demonstrated; (2) the rate of inactivation of enzymatic activity with the two substrates in 1.2 M NaCl was the same; (3) similar losses of hydrolytic activity with tri- and monooleoylglycerol were observed in the presence of low concentrations of n-butyl (p-nitrophenyl) carbamide; (4) inhibition of both hydrolytic activities by this compound could be prevented by prior exposure of lipoprotein lipase to either substrate.

Publishing year

1976

Language

English

Pages

1904-1909

Publication/Series

Biochemistry

Volume

15

Issue

9

Document type

Journal article

Publisher

The American Chemical Society (ACS)

Topic

  • Biochemistry and Molecular Biology

Status

Published

ISBN/ISSN/Other

  • ISSN: 0006-2960