Purification and Properties of a Lipase from Rat Adipose Tissue
J. T. Mann III 1 and S. B. Tove 1
From the
1 From the Nutritional Biochemistry Section, Department of Animal Science, North Carolina State University, Raleigh, North Carolina 27607
A highly purified lipase was prepared from the particulate fraction of rat adipose tissue. Although the lipase catalyzes the hydrolysis of diglycerides and triglycerides of both long and short chain fatty acids, monoglycerides are not hydrolyzed. The enzyme has a marked specificity toward fatty acids esterified to the primary hydroxyl groups and hydrolyzes
,ß-diglycerides 10 times more rapidly than
,
'-diglycerides. Thus, action of this enzyme would tend to promote the formation of ß-monoglycerides in adipose tissue and catalyze the exchange of free fatty acids at the
positions of the triglycerides of adipose tissue.
Submitted on August 27, 1965