Purification of a UTP: d-Glucose-1-phosphate uridylyl-transferase from Golgi apparatus of cat liver by affinity chromatography on UTP-agarose

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Abstract

UDP-glucose pyrophosphorylase from Golgi apparatus solubilized by detergent has been purified 100-fold from microsomes by affinity chromatography on UTP-agarose. The purified enzyme has apparent Mr 270,000 and isoelectric pH 3.9 against 360,000 and 4.2 for soluble enzyme. According to these characteristics, UDP-glucose pyrophosphorylase from Golgi apparatus is different from cytosolic enzyme. © 1984.

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Azzar, G., Persat, F., Degiuli, A., & Got, R. (1984). Purification of a UTP: d-Glucose-1-phosphate uridylyl-transferase from Golgi apparatus of cat liver by affinity chromatography on UTP-agarose. Analytical Biochemistry, 142(2), 518–520. https://doi.org/10.1016/0003-2697(84)90499-8

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