EFFECTS OF MONOOLEIN ON HYDROLYSIS OF TRIGLYCERIDE BY LIPOPROTEIN-LIPASE IN PRESENCE OF AN INHIBITORY APOLIPOPROTEIN

  • 1 January 1976
    • journal article
    • research article
    • Vol. 8  (3) , 197-206
Abstract
The previously demonstrated inhibition of cow''s milk lipoprotein lipase [EC 3.1.1.3] by apoLp-Ala [apolipoprotein with COOH-terminal Ala] and the deinhibition by monoglyceride were 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 purified lipase. The generation of monoglyceride may be important in facilitating hydrolysis of triglyceride in lipoproteins containing this inhibitory apolipoprotein.

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