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Effects of monoolein on hydrolysis of triglyceride by lipoprotein lipase in the presence of an inhibitory apolipoprotein.

Authors
Type
Published Article
Journal
Physiological chemistry and physics
0031-9325
Publication Date
Volume
8
Issue
3
Pages
197–206
Identifiers
PMID: 1034936
Source
Medline
License
Unknown

Abstract

The previously demonstrated inhibition of cow's milk lipoprotein lipase by apoLp-Ala and the deinhibition by monoglyceride have been studied in more detail. The apoLp-Ala inhibition is reversible by the addition of monoglyceride before or after enzyme additions. Quantities of monoglyceride accumulate during hydrolysis of triglyceride which are adequate to prevent inhibition by added apoLp-Ala. Accelerating reaction rates observed when the substrate contains the apoprotein at levels producing partial inhibition are also explained by monoglyceride production. These effects were observed with both crude preparations of skim milk and highly pruified lipase. It is suggested that the generation of monoglyceride may be important in facilitating hydrolysis of triglyceride in lipoproteins containing this inhibitory apolipoprotein.

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