Fluorescence study of a mutant cytochrome b5 with a single tryptophan in the membrane-binding domain.

@article{Ladokhin1991FluorescenceSO,
  title={Fluorescence study of a mutant cytochrome b5 with a single tryptophan in the membrane-binding domain.},
  author={Alexey S. Ladokhin and Ligong Wang and Allen W. Steggles and Peter W. Holloway},
  journal={Biochemistry},
  year={1991},
  volume={30 42},
  pages={
          10200-6
        }
}
Fluorescence studies of cytochrome b5 are complicated by the presence of three tryptophans, at positions 108, 109, and 112, in the membrane-binding domain. The cDNA for rabbit liver cytochrome b5, isolated from a lambda gt11 library, was used to generate a mutated mRNA where the codons for tryptophans-108 and -112 were replaced by codons for leucine. The sequence was expressed in Escherichia coli and the mutant protein was isolated. This mutant protein had the expected absorption spectrum, and… CONTINUE READING
BETA

Similar Papers