Abstract
Abstract Surface monolayer techniques have been applied to the study of lipoprotein lipase from lipid-free bovine milk. Lipoprotein lipase activity was determined by measurement of the decrease in surface radioactivity as a result of enzymic hydrolysis of a glyceryl tri[1-14C]octanoate monolayer. The rate of hydrolysis was enhanced 5-fold by 10 nm apolipoprotein glutamic acid from human very low density lipoprotein. The activator protein and the enzymic activity were shown to associate as a stable surface film in the absence of lipid.
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