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. 1987 Mar 15;242(3):923–926. doi: 10.1042/bj2420923

Studies on the biotin-binding site of avidin. Lysine residues involved in the active site.

G Gitlin, E A Bayer, M Wilchek
PMCID: PMC1147797  PMID: 3109401

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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