Title : The kinetics of heparin inhibition of the esterase and basal lipase activities of lipoprotein lipase.

Pub. Date : 1987 Mar

PMID : 3566288






3 Functional Relationships(s)
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1 On the other hand, the basal lipase activity of LPL against emulsified trioleoylglycerol (TG) was very sensitive to inhibition by heparin: 1 microgram/ml inhibited about 80% of the reaction and 3 micrograms/ml drove the reaction to zero. Triolein lipoprotein lipase Bos taurus
2 On the other hand, the basal lipase activity of LPL against emulsified trioleoylglycerol (TG) was very sensitive to inhibition by heparin: 1 microgram/ml inhibited about 80% of the reaction and 3 micrograms/ml drove the reaction to zero. Triolein lipoprotein lipase Bos taurus
3 It is concluded that TG and heparin as well as C-II and heparin are mutually exclusive and that lipoprotein lipase is a multisite enzyme, possibly a tetramer, with three high-affinity catalytic sites, and an equal number of sites for C-II and heparin per oligomer. Triolein lipoprotein lipase Bos taurus