Isolation and characterization of pig kidney mitochondrial ferredoxin:NADP+ oxidoreductase.
作者： W Gnanaiah , J L Omdahl
DOI: 10.1016/S0021-9258(18)67140-6
关键词:
摘要: A two-step affinity chromatography procedure, using 2',5'-ADP-agarose and adrenodoxin-Sepharose 4B supports, was used to purify mitochondrial ferredoxin:NADP+ oxidoreductase (EC 1.18.1.2, formerly EC 1.6.7.1) from pig kidney. The 450:270 nm absorbance ratio of the enzyme 0.128, it had a specific activity 16,305 nmol/min/mg for reduction cytochrome c. monomer which contained one molecule FAD calculated molecular masses 51,500 48,000 daltons when determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis high performance liquid exclusion chromatography, respectively. porcine Km NADPH 0.94 microM expressed maximal coupled with its homologous ferredoxin, although also active heterologous ferredoxin bovine adrenal. purified supported in vitro membrane-bound adrenal P-450, demonstrated immunologic studies that shares some common epitopes adrenodoxin:NADP+ oxidoreductase.
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