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- W201672746 abstract "A rapid method is described for the purification of galactose-1-phosphate uridylyltransferase (EC 2.7.7.12) from human red blood cells by the use of DEAE-cellulose and two steps of affinity chromatography on a uridine-aminohexyl agarose column. The enzyme consists of two identical subunits of 31,000 molecular weight as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Chromatography on Sephadex G-200 chromatography gave a molecular weight of 69,000 for the native enzyme, it being eluted from the column with bovine serum albumin. Cross-linking of the enzyme with dimethylsuberimidate followed by analysis of the products by sodium dodecyl sulfate polyacrylamide gel electrophoresis caused the near-disappearance of the 31,000 molecular weight subunit and the appearance of a protein with a molecular weight of about 65,000 without the appearance of higher polymers." @default.
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- W201672746 date "1976-02-01" @default.
- W201672746 modified "2023-10-18" @default.
- W201672746 title "Purification of normal and inactive galactosemic galactose-1-phosphate uridylyltransferase from human red cells." @default.
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- W201672746 doi "https://doi.org/10.1016/s0021-9258(17)33801-2" @default.
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