Corran P H, Waley S G
Biochem J. 1975 Aug;149(2):357-64. doi: 10.1042/bj1490357.
The mode of reaction of benzylpenicillin with two proteins was studied, with particular reference to the allergenicity of penicillin. These reactions, with pig insulin, and with hen's-egg-white lysozyme, were carried out in neutral solution at 37 degrees C. High concentrations of penicillin are needed to label the proteins, owing to concurrent hydrolysis of penicillin. Evidence has been obtained that the penicillin-reactive sites on the insulin molecule are the alpha-amino group at the N-terminus of the A chain and the epsilon-amino group of the lysine residue; whereas a site of reaction with lysozyme appears to be the epsilon-amino group of lysine-116.
研究了苄青霉素与两种蛋白质的反应模式,特别提及青霉素的致敏性。这些反应分别是在37℃的中性溶液中,苄青霉素与猪胰岛素以及与鸡蛋清溶菌酶之间进行的。由于青霉素会同时发生水解,因此需要高浓度的青霉素才能标记这些蛋白质。已经获得的证据表明,胰岛素分子上与青霉素反应的位点是A链N端的α-氨基以及赖氨酸残基的ε-氨基;而与溶菌酶反应的一个位点似乎是赖氨酸-116的ε-氨基。