Cytochrome-b5 reductase
Author:
Publisher
Springer Berlin Heidelberg
Link
http://link.springer.com/content/pdf/10.1007/3-540-37662-3_4.pdf
Reference67 articles.
1. Bonomi, F.; Long, R.C.; Kurtz, D.M.: Purification and properties of a membrane-bound NADH-cytochrome-b5 reductase from erythrocytes of the sipunculid worm, Phascolopsis gouldii. Biochim. Biophys. Acta, 999, 147–156 (1989)
2. Rigby, J.S.; Bull, P.C.; Ashworth, A.; Shephard, E.A.; Santisteban, I.; Phillips, I.R.: Isolation and characterization of genes coding for cytochrome b5 and cytochrome-b5 reductase. Biochem. Soc. Trans., 17, 194–195 (1989)
3. Palmieri, D.A.; Rangachari, A.; Butterfield, D.A.: Effects of domain-specific erythrocyte membrane modulators on acetylcholinesterase and NADH:cytochrome b5 reductase activities. Arch. Biochem. Biophys., 280, 224–228 (1990)
4. Tamura, M.; Yoshida, S.; Tamura, T.; Saitoh, T.; Takeshita, M.: Effect of divalent cations on NADH-dependent and NADPH-dependent cytochrome b5 reduction by hepatic microsomes. Arch. Biochem. Biophys., 280, 313–319 (1990)
5. Borgese, N.; Longhi, R.: Both the outer mitochondrial membrane and the microsomal forms of cytochrome b5 reductase contain covalently bound myristic acid. Quantitative analysis on the polyvinylidene difluoride-immobilized proteins. Biochem. J., 266, 341–347 (1990)
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