利用脱水胰凝乳蛋白酶 (保持天然酶的完整结合部位 ,但没有催化活性 )作为靶蛋白 ,在噬菌体肽库中钓取一些有结合活力噬菌体 ,再将得的噬菌体同固定化的天然酶一起保温 ,能够被天然酶水解的那部分噬菌体即为底物噬菌体 .利用 DNA测序技术测出筛得的短肽序列 ,分析序列保守性 ,发现 WR和 YF的组合具有很强的保守性 .合成相应的几个短肽 ,与天然酶作用 ,发现芳香族氨基酸与碱性氨基酸的组合较易被胰凝乳蛋白酶切割 .而且 ,当 P2 、P3 位置为侧链较小的氨基酸或碱性氨基酸时 ,更有利于水解的发生 .精氨酸无论处在任何位置 ,对水解往往都有促进作用 Using dehydrated chymotrypsin, which retains the intact binding site of the native enzyme but has no catalytic activity, as a target protein, some phage with binding activity are picked up from the phage peptide library and the resulting phage are incubated with the immobilized native enzyme , The part of the phage that can be hydrolyzed by the natural enzyme is the substrate bacteriophage.The DNA sequencing technique was used to detect the short peptide sequence and analyze the sequence conservation.The results showed that the combination of WR and YF was highly conserved.The corresponding Several short peptides interact with natural enzymes and found that the combination of aromatic amino acids and basic amino acids is more likely to be cleaved by chymotrypsin.Moreover, when the P2 and P3 positions are smaller amino acids or basic amino acids, Is conducive to the occurrence of hydrolysis arginine, whether in any position, often have a catalytic effect on hydrolysis