Purification and properties of triglyceride synthetase from the intestinal mucosa

Abstract

1. 1. Triglyceride synthetase from hamster intestinal mucosa has been purified approx. 70-fold. The synthetase contains acyl-CoA:monoglyceride acyl transferase, acyl-CoA:diglyceride acyl transf erase and acyl-CoA synthetase. These enzymes appear to be purified simultaneously. 2. 2. The synthetase exhibits maximal activity at pH 7.0–7.5. K m value for palmityl-CoA is 5.6 · 10 −5 M and for 2-monopalmitin 5.9 · 10 −5 M. 3. 3. The enzymatic activity is destroyed by exposure to a variety of detergents. 4. 4. Polyacrylamide-gel electrophoresis of the synthetase shows that it consists of four proteins. The one with the highest mobility stains for lipid and binds deoxycholate, monoglyceride and palmityl-CoA. 5. 5. Sucrose gradient centrifugation studies indicate that the substrates and products are enzyme-bound.