Title of article
UDP-glucose dehydrogenase from Capra hircus liver: Purification, partial characterization and evaluation as a coupling enzyme in UDP-galactose 4-epimerase assay
Author/Authors
Banerjee، نويسنده , , Nupur and Bhattacharyya، نويسنده , , Debasish، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2011
Pages
7
From page
37
To page
43
Abstract
UDP-glucose dehydrogenase from Capra hircus has been purified to homogeneity by salt fractionations, heat treatment and chromatographic steps. It is a homohexamer of about 300 kDa. Though the basic physical and enzymatic properties of the caprine enzyme are comparable to those of the beef liver enzyme, it has lower energy of activation and different entropy and enthalpy for the transition state during catalysis. The caprine enzyme can act suitably as an auxiliary enzyme in the coupled assay system for UDP-galactose 4-epimerase.
s: UDP-Glc DH, UDP-glucose dehydrogenase (EC 1.1.1.22); Epimerase, UDP-galactose 4-epimerase (EC 5.1.3.2).
Keywords
UDP-glucose dehydrogenase , Caprine liver , enzyme purification , UDP-galactose 4-epimerase , Coupled enzyme assay , enzyme stability
Journal title
Journal of Molecular Catalysis B Enzymatic
Serial Year
2011
Journal title
Journal of Molecular Catalysis B Enzymatic
Record number
1716876
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