Studies on the biotin-binding site of avidin. Lysine residues involved in the active site
- 15 March 1987
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 242 (3), 923-926
- https://doi.org/10.1042/bj2420923
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.This publication has 10 references indexed in Scilit:
- A sensitive enzyme assay for biotin, avidin, and streptavidinAnalytical Biochemistry, 1986
- Molecular cloning and nucleotide sequence of the streptavidin geneNucleic Acids Research, 1986
- The occurrence and production of avidin: a new conception of the high-affinity biotin-binding proteinComparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1984
- The Use of the Avidin‐Biotin Complex as a Tool in Molecular BiologyPublished by Wiley ,1980
- AvidinAdvances in protein chemistry, 1975
- Egg white avidin. 3. Sequence of the 78-residue middle cyanogen bromide peptide. Complete amino acid sequence of the protein subunit.1971
- AVIDIN. 3. THE NATURE OF THE BIOTIN-BINDING SITEBiochemical Journal, 1963
- Relation between modification of functional groups of proteins and their biological activity. I.A graphical method for the determination of the number and type of essential groups.1962
- Spectroscopic evidence for the participation of tryptophan residues in the binding of biotin by avidinBiochimica et Biophysica Acta, 1962
- Avidin. II. Composition and mode of action of avidin AArchives of Biochemistry and Biophysics, 1952