Studies on the biotin-binding site of avidin. Lysine residues involved in the active site.
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.
D000596:Amino Acids / Q000032:analysis; D001360:Avidin / Q000378:metabolism*; D001665:Binding Sites; D001710:Biotin / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D008239:Lysine / Q000032:analysis; D010446:Peptide Fragments / Q000032:analysis
D000596:Amino Acids; D010446:Peptide Fragments; D001360:Avidin; D001710:Biotin; D008239:Lysine