Human galactose-1-phosphate uridylyltrsferase: purification and comparison of the red blood cell and placental enzymes |
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| Authors: | V P Williams G R Helmer C Fried |
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| Affiliation: | Department of Psychiatry, Mental Retardation Research Center, University of California Los Angeles, School of Medicine, Los Angeles, California 90024 U.S.A. |
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| Abstract: | Galactose-1-phosphate Uridylyltransferase (uridine diphosphoglucose: α-d-galactose-1-phosphate Uridylyltransferase, EC 2.7.7.12) has been purified from human red blood cells and placental tissue. The placental enzyme was obtained as a homogeneous protein with a specific activity of about 100 units/mg of protein by a combination of previously published methods (G. R. Helmer, Jr., and V. P. Williams, 1981,Arch. Biochem. Biophys.210, 573–580) and concanavalin A-Sepharose chromatography. The properties of the two enzyme forms have been examined with respect to subunit size, electrophoretic properties, isozyme distribution, kinetic patterns, and immunological properties. |
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| Keywords: | To whom correspondence should be sent. |
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