Gitlin G, Bayer E A, Wilchek M
Biochem J. 1987 Mar 15;242(3):923-6. doi: 10.1042/bj2420923.
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.
用1-氟-2,4-二硝基苯处理蛋清抗生物素蛋白。每个抗生物素蛋白亚基平均一个赖氨酸残基的修饰导致生物素结合能力完全丧失。从2,4-二硝基苯基化的抗生物素蛋白获得的胰蛋白酶肽通过反相高效液相色谱进行分离。三个肽含有2,4-二硝基苯基。氨基酸分析表明，赖氨酸残基45、94和111被修饰，可能构成生物素结合位点的一部分。
