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. 1988 Feb 15;250(1):291–294. doi: 10.1042/bj2500291

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

G Gitlin 1, E A Bayer 1, M Wilchek 1
PMCID: PMC1148846  PMID: 3355517

Abstract

Egg-white avidin was modified with the tryptophan-specific reagent 2-hydroxy-5-nitrobenzyl bromide. The complete loss of biotin-binding activity was achieved upon modification of an average of one tryptophan residue per avidin subunit. The identity of the modified residues was determined by isolating the relevant tryptic and chymotryptic peptides from CNBr-cleaved avidin fragments. The results demonstrate that Trp-70 and Trp-110 are modified in approximately equivalent proportions. It is believed that these residues are located in the active site of avidin and take part in the binding of biotin.

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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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