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Studies on metabolism of tri glyceride in hepato biliary disorders 3. partial purification and characterization of tri glyceride lipase from rat liver



Studies on metabolism of tri glyceride in hepato biliary disorders 3. partial purification and characterization of tri glyceride lipase from rat liver



Acta Scholae Medicinalis Universitatis in Gifu 29(3): 507-514



Hepatic triglyceride lipase (H-TGL) was extracted from the rat liver with 0.05 M NH4Cl-NH4 OH buffer (pH 8.5) containing 0.5 U/ml of heparin for 60 min at 0.degree. C. The crude enzyme extracts obtained were partially purified by means of a heparin-Sepharose affinity chromatography. This gave a 78-fold purification over the crude enzyme extracts. The purified enzyme did not require serum for substrate activation and was not inhibited by 1 M NaCl, being different from lipoprotein lipase (LPL) in rat postheparin plasma. The purified enzyme had a single pH optimum at 9.0, whereas the crude enzyme extracts had lipolyptic activities over a wide range of pH values, having 2 maxima at pH 9.0 and 4.0. The lipolyptic activities in the crude enzyme extracts were separated on heparin-Sepharose column into 2 fractions; a breakthrough fraction and a purified H-TGL. In an attempt to define the localization of these lipolytic activities, NaCl-noninhibitable H-TGL in postheparin plasma and crude enzyme extracts of postheparin liver were assayed for their activities at different pH values. The lipolytic activities of the crude extracts of postheparin liver had a pH optimum at 4.0 with a marked decrease at 9.0 being the same as that of the breakthrough fraction of the column. Heparin-released H-TGL in plasma had a similar pH dependence to that of a purified H-TGL. TG lipase activity in the liver is evidently heterogeneous. This enzyme activity can be separated into 2 forms: One, having a high affinity for heparin bound to Sepharose, is present in the hepatic plasma membrane and released by heparin onto the circulation. The other, having no affinity for heparin, might be present in the intracellular compartment.

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