The binding of deoxycholate, Triton X-100, sodium dodecyl sulfate, and phosphatidylcholine vesicles to cytochrome b5.

@article{Robinson1975TheBO,
  title={The binding of deoxycholate, Triton X-100, sodium dodecyl sulfate, and phosphatidylcholine vesicles to cytochrome b5.},
  author={Neal C. Robinson and Charles Tanford},
  journal={Biochemistry},
  year={1975},
  volume={14 2},
  pages={369-78}
}
Cytochrome b5 is composed of two domains that can be isolated after tryptic cleavage as two polypeptide fragments. One fragment is globular and hydrophilic and contains the heme; the other fragment is rich in hydrophobic amino acids and is essential for recombination of cytochrome b5 with microsomal membranes (Ito, A., and Sato, R. (1968), J. Biol. Chem. 243, 4922; Spatz, L., and Strittmatter, P. (1971), Proc. Nat. Acad. Sci. U.S. 68, 1042). Equilibrium dialysis and sedimentation equilibrium… CONTINUE READING

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