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PMID: 3109401 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

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

The Biochemical journal ·Vol. 242 ·No. 3 ·1987-03-15 ·Pages 923-6

Gitlin G, Bayer EA, Wilchek M

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.

MeSH Terms

Amino Acids/analysis Avidin/metabolism Binding Sites Biotin/metabolism Chromatography, High Pressure Liquid Lysine/analysis Peptide Fragments/analysis

Chemicals

Amino Acids Peptide Fragments Avidin Biotin Lysine

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Gitlin G

Bayer E A

Wilchek M

References (10)

10 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj2420923

Published

1987-03-15

Pages

923-6

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1147797

Subset

External Links

PubMed source DOI: 10.1042/bj2420923 PMC Full Text View journal details

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

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