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  • Title: Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin.
    Author: Hadváry P, Lengsfeld H, Wolfer H.
    Journal: Biochem J; 1988 Dec 01; 256(2):357-61. PubMed ID: 3223916.
    Abstract:
    Tetrahydrolipstatin inhibits pancreatic lipase from several species, including man, with comparable potency. The lipase is progressively inactivated through the formation of a long-lived covalent intermediate, probably with a 1:1 stoichiometry. The lipase substrate triolein and also a boronic acid derivative, which is presumed to be a transition-state-form inhibitor, retard the rate of inactivation. Therefore, in all probability, tetrahydrolipstatin reacts with pancreatic lipase at, or near, the substrate binding or active site. Tetrahydrolipstatin is a selective inhibitor of lipase; other hydrolases tested were at least a thousand times less potently inhibited.
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