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Article

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

Biochemistry - 22 Oct 1991

Ladokhin A S, Wang L, Steggles A W, Holloway P W

Abstract excerpt

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...

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PMID: 1931948
DOI: 10.1021/bi00106a018

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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