Some properties of the apoenzyme of NADPH-adreno-ferredoxin reductase from bovine adrenocortical mitochondria.
作者信息
Yamazaki M, Ichikawa Y
机构信息
Department of Biochemistry, Kagawa Medical School, Japan.
出版信息
Int J Biochem. 1990;22(10):1147-52. doi: 10.1016/0020-711x(90)90113-h.
PMID:2289620
Abstract
- An apo-NADPH-adreno-ferredoxin reductase (EC 1.18.1.2) was obtained from bovine adrenocortical mitochondria and its physicochemical properties were investigated. 2. The effects of various substances such as NADPH, FAD and adreno-ferredoxin on the interaction of the apo-reductase were investigated by various column chromatographies. 3. The apo- and holo-reductases were found to be separated by adreno-ferredoxin affinity chromatography. 4. The removal of FAD from NADPH-adreno-ferredoxin reductase did not affect the net charge of the reductase. 5. The values of s20,w of apo- and holo-reductases were 3.8 x 10(-13) sec and 3.9 x 10(-13) sec, respectively. 6. The apo-reductase was more easily denatured by heat treatment than the holo-reductase. 7. FAD, and adreno-ferredoxin and both could protect the apo-reductase from thermal inactivation.
摘要
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