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May 1, 1982Journal of Biological ChemistryOpen Access

Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region.

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Authors

SBShaun D. BlackThe University of Texas at TylerMCMinor J. CoonUniversity of Illinois Urbana-Champaign

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Black et al. (1982) studied this question.

synapsesocial.com/papers/69d7ecfb11d83f35e5ae34b9https://doi.org/10.1016/s0021-9258(19)83868-1
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Interactions of cytochrome P-450, NADPH-cytochrome P-450 reductase, phospholipid, and substrate in the reconstituted liver microsomal enzyme system.1980 · 226 citations
  2. 2Cytochrome b5 from microsomal membranes of equine, bovine, and porcine livers. Isolation and properties of preparations containing the membranous segment1974 · 116 citations
  3. 3Empirical Predictions of Protein Conformation1978 · 3,145 citations
  4. 4Application of 0.1 M quadrol to the microsequence of proteins and the sequence of tryptic peptides1975 · 395 citations
  5. 5Isolation of the membrane-binding peptide of NADPH-cytochrome P-450 reductase. Characterization of the peptide and its role in the interaction of reductase with cytochrome P-450.1981 · 56 citations