Abstract
1. Lysosomal MU-oleate hydrolase (MUH) from rabbit liver was partially purified by Sephadex LH-20, DEAE Sephadex A-50, Bio-Gel A-5m, hydroxyapatite column chromatography.2. The enzyme was compared with other lipolytic enzymes such as acid cholesteryl esterase (ACE), triglyceride lipase (TGL) in this paper. The heat-sensitivity and other properties of both MUH and ACE were very similar.3. MUH was activated by lysosome-rich fraction and the structure of lysosomal membrane might require for the capacity of activation.4. MUH activity against enzyme concentration exhibited sigmoidal curve which suggested that MUH might be membrane associated enzyme and it might be activated by itself.
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