Immunoaffinity purification and characterization of mitochondrial membrane-bound D-3-hydroxybutyrate dehydrogenase from Jaculus orientalis

Table 1 Purification steps of BDH from jerboa liver

	Total protein (mg)	Specific activity (nmol/min/mg of protein)	Total activity (μmol/min)	Purification factor (fold)	Yield (%)
Crude extract	5100	1.1	5.5	1.0	100
Ammonium sulphate (30–50%)	560*	8.2	4.5	7.4	82
Phenyl-Sepharose	350	10.4	3.6	9.4	65
Sepharose-Blue	50	17.6	0.87	16.0	16
Immunoaffinity chromatography	0.75	41.3	0.030	37.5	0.50

Typical experiments were reported from three independent trials.
* The ammonium sulphate precipitation step eliminates 91% of contaminating proteins from Jerboa crude extracts, respectively. These values were calculated from the total protein amount deduced from the amount of BDH (estimated from specific activities after the immunoaffinity chromatography step).

ISSN: 1471-2091