scholarly journals Purification and characterization of malate dehydrogenase from sheep liver (Ovis aries): Application in AST assay diagnostic kit

2018 ◽  
Keyword(s):  
Malate Dehydrogenase ◽  
Ovis Aries ◽  
Purification And Characterization ◽  
Sheep Liver

Cloning, Expression, Purification, and Characterization of the 6-Phosphogluconate Dehydrogenase from Sheep Liver

1998 ◽  
Vol 13 (2) ◽  
pp. 251-258 ◽  
Author(s):  
Lilian Chooback ◽  
Nancy E. Price ◽  
William E. Karsten ◽  
John Nelson ◽  
Paula Sundstrom ◽  
...  
Keyword(s):  
Purification And Characterization ◽  
Phosphogluconate Dehydrogenase ◽  
Sheep Liver

Purification and Characterization of Membrane-bound Malate Dehydrogenase fromAcetobactersp. SKU 14

2002 ◽  
Vol 66 (2) ◽  
pp. 298-306 ◽  
Author(s):  
Emiko SHINAGAWA ◽  
Terumi FUJISHIMA ◽  
Duangtip MOONMANGMEE ◽  
Gunjana THEERAGOOL ◽  
Hirohide TOYAMA ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Purification And Characterization ◽  
Membrane Bound

scholarly journals Purification and Characterization of Xanthine Oxidase from Liver of the Sheep (Ovis Aries)

2019 ◽  
Vol 1 (4) ◽  
pp. 8-18
Author(s):  
Samir A.M. Zaahkouk ◽  
Doaa A. Darwish ◽  
Hassan M.M. Masoud ◽  
Mohamed M. Abdel-Monsef ◽  
Mohamed S. Helmy ◽  
...  
Keyword(s):  
Xanthine Oxidase ◽  
Specific Activity ◽  
Deae Cellulose ◽  
Ovis Aries ◽  
Major Band ◽  
Sheep Liver ◽  
Sds Page ◽  
Commercially Important ◽  
Important Enzyme

Xanthine oxidase is a commercially important enzyme with wide area of medical applications to develop diagnostic kits. Xanthine oxidase was extracted, purified and characterized from sheep liver (SLXO). The purification procedure involved acetone precipitation and chromatography on DEAE-cellulose and Sephacryl S-300 columns. The sheep liver xanthine oxidase was homogeneously purified 31.8 folds with 3.5 U/mg specific activity and 24.1% recovery. SLXO native molecular weight was 150 kDa and on SDS-PAGE appeared as single major band of 75 kDa representing a homodimer protein. Isoelectric focusing of the purified SLXO resolved into two closely related isoforms with pI values of 5.6 and 5.8. The apparent Km for xanthine oxidase at optimum pH 7.6 was found to be 0.9 mM xanthine. FeCl2 and NiCl2 increased the activity of SLXO, while CuCl2 and ZnCl2 were found to be potent inhibitors of the purified enzyme. Allopurinol inhibits SLXO competitively with one binding site on the purified molecule and Ki value of 0.06 mM.

PURIFICATION AND CHARACTERIZATION OF A MALATE DEHYDROGENASE FROM PHASEOLUS MUNGO

2005 ◽  
Vol 29 (2) ◽  
pp. 117-131 ◽  
Author(s):  
SHAOYUN WANG ◽  
ZHIBIN XU ◽  
XIUYUN YE ◽  
PINGFAN RAO
Keyword(s):  
Malate Dehydrogenase ◽  
Purification And Characterization ◽  
Phaseolus Mungo

Purification and characterization of the individual glutathione S-transferases from sheep liver

1983 ◽  
Vol 224 (1) ◽  
pp. 87-101 ◽  
Author(s):  
C.Channa Reddy ◽  
John R. Burgess ◽  
Zhen-Zhen Gong ◽  
Edward J. Massaro ◽  
Chen-Pei D. Tu
Keyword(s):  
Purification And Characterization ◽  
Sheep Liver ◽  
Glutathione S Transferases ◽  
The Individual
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