Purification and Properties of Uridine Diphosphoglucose 4-epimerase from Escherichia coli*
- 1 August 1964
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 56 (2) , 138-144
- https://doi.org/10.1093/oxfordjournals.jbchem.a127970
Abstract
A method for purification of UDPglucose 4-epimerase from Escherichia coli was described. An overall purification of 80-fold above the crude extract was achieved. With the use of this partially purified enzyme preparation, some of its properties were studied. The Km value is 1.6×10−4M for UDPgalactose and 1.0×10−3M for UDPglucose. The enzyme has a broad pH optimum between 7.5 and 9.0. This enzyme does not require a catalytic amount of NAD for its reaction, and the enzyme activity is not inhibited by p-chloromercuribenzoate.Keywords
This publication has 7 references indexed in Scilit:
- HEREDITARY DEFECTS IN GALACTOSE METABOLISM IN ESCHERICHIA COLI MUTANTS, I. DETERMINATION OF ENZYME ACTIVITIESProceedings of the National Academy of Sciences, 1959
- Yeast uridine diphosphogalactose-4-epimerase, correlation between activity and fluorescenceArchives of Biochemistry and Biophysics, 1958
- THE ENZYMIC INTERCONVERSION OF URIDINE DIPHOSPHOGALACTOSE AND URIDINE DIPHOSPHOGLUCOSEJournal of Biological Chemistry, 1957
- ENZYMATIC FORMATION OF URIDINE DIPHOSPHOGLUCURONIC ACIDJournal of Biological Chemistry, 1957
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- The enzymatic transformation of uridine diphosphate glucose into a galactose derivativeArchives of Biochemistry and Biophysics, 1951
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934