UDP-glucose dehydrogenase from Escherichia coli. Purification and subunit structure.
UDPglucose dehydrogenase from Escherichia coli has been purified 330-fold with an overall yield of 27%. A single homogeneous subunit was demonstrated by ultracentrifugation in 6 M guanidium chloride and by dodecyl sulfate-polyacrylamide gel electrophoresis. Since the molecular weight of the intact dehydrogenase is in the order of 86 000 and the subunit weight determined by the dodecyl sulfate-polyacrylamide gel electrophoresis is 47 000, the enzyme consists of two polypeptide chains. The sole amino terminal acid shown by the dansylation technique was arginine. Forty-four tryptic peptides were obtained by peptide mapping, in agreement with the number of arginine and lysine residues/mole protein [43] determined by amino acid analysis. The data are consistent with the presence of two identical or very similar polypeptide chains in E. coli UDPglucose dehydrogenase.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D004355:Drug Stability; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D013053:Spectrophotometry; D014533:Uridine Diphosphate Glucose Dehydrogenase / Q000302:isolation & purification
D000596:Amino Acids; D046911:Macromolecular Substances; D010446:Peptide Fragments; D000429:Alcohol Oxidoreductases; D014533:Uridine Diphosphate Glucose Dehydrogenase