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Purification And Characterization Of Lipoprotein Lipase From Rat Brown Fat

D. Guerrier, H. Pellet
Published 1979 · Biology, Medicine

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The lipoprotein lipase (EC 3.1 .1.34) is a major factor in the uptake of chylomicrons and very low density lipoprotein triglycerides by extrahepatic tissues. It has been purified from various sources [l-7] by affinity chromatography on heparin-Sepharose. Brown adipose tissue present in hibernating mammals, but also in homeotherm mammals, including Man, where it is particularly developed in the new-born, plays a very important role in nonshivering thermogenesis. The latter is particularly active at birth, in animals exposed to the cold and during the waking period following hibernation. Lipoprotein lipase, by enabling the energy substrates (free fatty acids) necessary for heat production to enter the brown fat cell, appears as a key enzyme controlling for a large part the calorigenic possibilities of this tissue. However, little work [8--l l] has been devoted to the study of brown fat LPL and no purification assay has been made. In this work, we describe for the first time a highly purified preparation of LPL obtained from rat brown fat. We have studied the extraction and stability of the enzyme as compared with rat heart and in relation to the presence of NaCl (in the extraction buffer), purification on heparin-Sepharose and finally the properties of the purified enzyme.
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