Purification of muscle uridine diphosphoglucose pyrophosphorylase by hydrophobic chromatography.
Uridine diphosphoglucose pyrophosphorylase was purified 2500-fold from rabbit skeletal muscle with a total recovery of 35% of the initial activity. The present procedure was made possible by an extensive use of hydrophobic chromatography. Purified pyrophosphorylase had a specific activity of 500 mumol/min/mg of protein and was homogeneous by chromatographic and electrophoretic criteria. The enzyme appears to be composed of eight subunits of 53,000 molecular weight each.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002845:Chromatography / Q000379:methods; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D009713:Nucleotidyltransferases / Q000302:isolation & purification*; D011817:Rabbits; D013053:Spectrophotometry; D005957:UTP-Glucose-1-Phosphate Uridylyltransferase / Q000302:isolation & purification*
D000596:Amino Acids; D009713:Nucleotidyltransferases; D005957:UTP-Glucose-1-Phosphate Uridylyltransferase