Purification and Properties of Uridine Diphosphoglucose 4-epimerase from <i>Escherichia coli</i>

• IMAE YASUO

  Institute for Protein Research, Osaka University

• MORIKAWA NOBUKO

  Institute for Protein Research, Osaka University

• KURAHASHI KIYOSHI

  Institute for Protein Research, Osaka University

抄録

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.<br> With the use of this partially purified enzyme preparation, some of its properties were studied.<br> The K_m value is 1.6×10^-4M for UDP-galactose and 1.0×l0^-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.

収録刊行物

• The Journal of Biochemistry

  The Journal of Biochemistry 56 (2), 138-144, 1964

  The Japanese Biochemical Society

詳細情報

• CRID: 1571417128104352768
• NII論文ID: 130003537181
• ISSN: 0021924X
• Web Site: https://jlc.jst.go.jp/DN/JALC/00339893205?from=CiNii
• 本文言語コード: en
• データソース種別:
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