| Literature DB >> 3109401 |
G Gitlin, E A Bayer, M Wilchek.
Abstract
Egg-white avidin was treated with 1-fluoro-2,4-dinitrobenzene. Modification of an average of one lysine residue per avidin subunit caused the complete loss of biotin binding. Tryptic peptides obtained from the 2,4-dinitrophenylated avidin were fractionated by reversed-phase h.p.l.c. Three peptides contained the 2,4-dinitrophenyl group. Amino acid analysis revealed that lysine residues 45, 94 and 111 are modified and probably comprise part of the biotin-binding site.Entities:
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Year: 1987 PMID: 3109401 PMCID: PMC1147797 DOI: 10.1042/bj2420923
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857