Matsushima A, Okada M, Inada Y
FEBS Lett. 1984 Dec 10;178(2):275-7. doi: 10.1016/0014-5793(84)80615-8.
Chymotrypsin was modified in the zymogen form with 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine (activated PEG2), followed by activation with trypsin. The modified enzyme was soluble in benzene and retained its enzymic activity. Acid-amide bond formation by the modified enzyme proceeded efficiently in benzene: N-benzoyltyrosine butylamide was made from N-benzoyl-L-tyrosine ethyl ester and n-butylamine, and benzoyltyrosine(oligo)phenylalanine ethyl esters were formed from N-benzoyl-L-tyrosine ethyl ester and L-phenylalanine ethyl ester.
用2,4-双（O-甲氧基聚乙二醇）-6-氯-s-三嗪（活化的PEG2）将胰凝乳蛋白酶以酶原形式进行修饰，随后用胰蛋白酶激活。修饰后的酶可溶于苯并保留其酶活性。修饰后的酶在苯中能高效地进行酰胺键形成反应：由N-苯甲酰-L-酪氨酸乙酯和正丁胺合成N-苯甲酰酪氨酸丁酰胺，由N-苯甲酰-L-酪氨酸乙酯和L-苯丙氨酸乙酯形成苯甲酰酪氨酸（寡聚）苯丙氨酸乙酯。
