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CYB5R3  -  cytochrome b5 reductase 3

Bos taurus

 
 
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High impact information on LOC515773

 

Biological context of LOC515773

 

Anatomical context of LOC515773

 

Associations of LOC515773 with chemical compounds

  • Thus, the membrane-binding domain of cytochrome b5 reductase is localized at the NH2-terminus of the whole protein [6].
  • Identification of the NH2-terminal blocking group of NADH-cytochrome b5 reductase as myristic acid and the complete amino acid sequence of the membrane-binding domain [12].
  • The diaphorase activity in the NADPH-cytochrome c reductase-containing portion is not dependent upon the presence of an amphiphile or phospholipid and is not associated with O2- generation [9].
  • This monolayer was without cytochemical peroxidase and diaphorase (NADPH reoxidation) activity [13].
  • Although p-iodonitrotetrazolium (INT) has frequently been used as a probe of the diaphorase activity of the neutrophil flavocytochrome b, the propensity of its radical to interact reversibly with O2 led us to question its specificity [14].
 

Physical interactions of LOC515773

 

Other interactions of LOC515773

 

Analytical, diagnostic and therapeutic context of LOC515773

References

  1. Properties of NADH-cytochrome-b5 reductase from human neutrophils. Badwey, J.A., Tauber, A.I., Karnovsky, M.L. Blood (1983) [Pubmed]
  2. Characterization of lysyl residues of NADH-cytochrome b5 reductase implicated in charge-pairing with active-site carboxyl residues of cytochrome b5 by site-directed mutagenesis of an expression vector for the flavoprotein. Strittmatter, P., Kittler, J.M., Coghill, J.E., Ozols, J. J. Biol. Chem. (1992) [Pubmed]
  3. Characterization of the role of lysine 110 of NADH-cytochrome b5 reductase in the binding and oxidation of NADH by site-directed mutagenesis. Strittmatter, P., Kittler, J.M., Coghill, J.E. J. Biol. Chem. (1992) [Pubmed]
  4. Identification of the essential cysteine residue of NADH-cytochrome b5 reductase. Hackett, C.S., Novoa, W.B., Ozols, J., Strittmatter, P. J. Biol. Chem. (1986) [Pubmed]
  5. Complete amino acid sequence of steer liver microsomal NADH-cytochrome b5 reductase. Ozols, J., Korza, G., Heinemann, F.S., Hediger, M.A., Strittmatter, P. J. Biol. Chem. (1985) [Pubmed]
  6. Isolation and partial characterization of the NH2-terminal membrane-binding domain of NADH-cytochrome b5 reductase. Kensil, C.R., Hediger, M.A., Ozols, J., Strittmatter, P. J. Biol. Chem. (1983) [Pubmed]
  7. Respiratory burst of rabbit peritoneal neutrophils. Transition from an NADPH diaphorase activity to an .O2(-)-generating oxidase activity. Laporte, F., Doussiere, J., Vignais, P.V. Eur. J. Biochem. (1990) [Pubmed]
  8. Structural comparison of bovine erythrocyte, brain, and liver NADH-cytochrome b5 reductase by HPLC mapping. Tamura, M., Yubisui, T., Takeshita, M., Kawabata, S., Miyata, T., Iwanaga, S. J. Biochem. (1987) [Pubmed]
  9. Purified leukocyte cytochrome b558 incorporated into liposomes catalyzes a cytosolic factor dependent diaphorase activity. Li, J., Guillory, R.J. Biochemistry (1997) [Pubmed]
  10. Relationship between appearance of GABA, fluorogenic monoamines and cytochrome oxidase activity during prenatal morphogenesis of chick myenteric plexus. Fekete, E., Gábriel, R., Boros, A. Anat. Embryol. (1991) [Pubmed]
  11. Expression of a low-molecular-weight (10 kDa) calcium binding protein in glial cells of the brain of the trout (Teleostei). Manso, M.J., Becerra, M., Becerra, M., Anadón, R. Anat. Embryol. (1997) [Pubmed]
  12. Identification of the NH2-terminal blocking group of NADH-cytochrome b5 reductase as myristic acid and the complete amino acid sequence of the membrane-binding domain. Ozols, J., Carr, S.A., Strittmatter, P. J. Biol. Chem. (1984) [Pubmed]
  13. Measurement of low concentrations of bovine thyrotrophin by iodide uptake and organification in porcine thyrocytes. Reader, S.C., Davison, B., Ratcliffe, J.G., Robertson, W.R. J. Endocrinol. (1985) [Pubmed]
  14. Exploration of the diaphorase activity of neutrophil NADPH oxidase. Poinas, A., Gaillard, J., Vignais, P., Doussiere, J. Eur. J. Biochem. (2002) [Pubmed]
  15. The interaction of NADH-cytochrome b5 reductase and cytochrome b5 bound to egg lecithin liposomes. Rogers, M.J., Strittmatter, P. J. Biol. Chem. (1975) [Pubmed]
  16. Cobalt and ruthenium replacement for iron in adrenal iron-sulfur protein (adrenodoxin). Preparation and some properties. Sugiura, Y., Ishizu, K., Kimura, T. Biochemistry (1975) [Pubmed]
  17. Purification of bovine liver microsomal NADH-cytochrome b5 reductase using affinity chromatography. Schafer, D.A., Hultquist, D.E. Biochem. Biophys. Res. Commun. (1980) [Pubmed]
 
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