Abstract
Lipases [EC 3.1.1.3] of rat liver and adipose tissue readily hydro-lyzed methyl butyrate in solution and the extent of hydrolysis did not increase in over-saturated solutions. It was demonstrated that the α-monomyristin-splitting activities of rat adipose tissue lipase and esterase and of liver lipase were competitively inhibited by α-monobutyrin. The Ediol, methyl butyrate, α-monomyristin and tributyrin splitting activities of purified liver lipase were precipitated by liver esterase antibody. Liver lipase was converted into the esterase by treatment with acetone or pancreatic lipase. Liver esterase was partly converted into the lipase by sonication with lipid. From these results, it was suggested that liver lipase is a complex of liver esterase and lipid.
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