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
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
Journal title :
Journal of Molecular Catalysis B Enzymatic