Purification and Properties of Uridine Diphosphoglucose 4-epimerase from Escherichia coli

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 1.6×10−4 M for UDPgalacto...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1964-08, Vol.56 (2), p.138-144
Main Authors: IMAE, YASUO, MORIKAWA, NOBUKO, KURAHASHI, KIYOSHI
Format: Article
Language:English
Subjects:
Ammonium Compounds
Benzoates
Calcium Phosphates
Centrifugation
Chemistry Techniques, Analytical
Chloromercuribenzoates
Chromatography
Escherichia coli
Gels
Hot Temperature
Isomerases
NAD
Nucleic Acids
Old Medline
Quaternary Ammonium Compounds
Racemases and Epimerases
Uridine Diphosphate Glucose
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Summary: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 1.6×10−4 M for UDPgalactose and 1.0×10−3 M 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.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a127970