Properties of crystalline reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase from bovine adrenocortical mitochonria. I. Physicochemical properties of holo- and apo-NADPH-adrenodoxin reductase and interaction between non-heme iron proteins and the reductase.

@article{Hiwatashi1976PropertiesOC,
  title={Properties of crystalline reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase from bovine adrenocortical mitochonria. I. Physicochemical properties of holo- and apo-NADPH-adrenodoxin reductase and interaction between non-heme iron proteins and the reductase.},
  author={Akio Hiwatashi and Yusuke Ichikawa and N Maruya and T. Nakajima M. Yamano and Kenji Aki},
  journal={Biochemistry},
  year={1976},
  volume={15 14},
  pages={3082-90}
}
A crystalline NADPH-adrenodoxin reductase was obtained from bovine adrenocortical mitochondria and its properties were investigated. Its molecular weights and isoelectric point were estimated to be 51 000 and 5.4, respectively. Amino acid and sugar contents and the interaction between the apo-reductase and flavin of NADPH-adrenodoxin reductase were investigated. Formation of a complex of bovine NADPH-adrenodoxin reductase with adrenodoxin, its apoadrenodoxin, or other non-heme iron proteins… CONTINUE READING