Abstract
1. 1. Human lipoprotein lipase has been purified 16 000-fold from post-heparin plasma. The product shows no activity against triglyceride in the absence of added lipoprotein. 2. 2. The enzyme is active against both diglyceride and monoglyceride emulsions in the absence of lipoprotein, but monoglyceride hydrolase activity requires the presence of either deoxycholate or unesterified fatty acid. 3. 3. The rate of enzyme activity is strongly dependent upon the identity of the lipoprotein present. 4. 4. The temperature optimum of enzyme activity is also significantly dependent upon the nature of the lipoprotein co-factor.
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