Kaye N M, Jollès P
Mol Cell Biochem. 1978 Aug 16;20(3):173-82. doi: 10.1007/BF00243764.
Bovine fibrinogen and the Aalpha and Bbeta chains of bovine fibrinogen have been subjected to chemical modification by a number of reagents and the effects of these procedures on the susceptibility of the proteins to thrombin hydrolysis is described. The reagents used were rose bengal (for photo-oxidation), 2-hydroxy-5-nitrobenzyl bromide, N-acetylimidazole, iodoacetic acid and diethyl pyrocarbonate. Evidence is presented which indicates that the tryptophan and tyrosine residues of fibrinogen are not involved to any great extent in the interaction of this protein with thrombin. Modification with iodoacetic acid suggests that methionine residues play a major role in such interactions, but the fibrinogen chains on which the important residues reside remain uncertain. The use of diethyl pyrocarbonate indicates the participation also of histidine in fibrinogen-thrombin interactions and that, whereas the histidine residues of the Bbeta chain are involved to a great extent, it appears that those of the Aalpha chain are not. The similarities which exist between the fibrinogen-thrombin and the kappa-casein-chymosin systems are discussed.
牛纤维蛋白原以及牛纤维蛋白原的αA链和βB链已用多种试剂进行了化学修饰，并描述了这些操作对蛋白质对凝血酶水解敏感性的影响。所用试剂为孟加拉玫瑰红（用于光氧化）、2-羟基-5-硝基苄基溴、N-乙酰咪唑、碘乙酸和焦碳酸二乙酯。有证据表明，纤维蛋白原的色氨酸和酪氨酸残基在该蛋白质与凝血酶的相互作用中没有很大程度的参与。碘乙酸修饰表明甲硫氨酸残基在这种相互作用中起主要作用，但重要残基所在的纤维蛋白原链仍不确定。焦碳酸二乙酯的使用表明组氨酸也参与了纤维蛋白原与凝血酶的相互作用，并且，虽然βB链的组氨酸残基在很大程度上参与其中，但αA链的组氨酸残基似乎没有参与。讨论了纤维蛋白原 - 凝血酶系统和κ-酪蛋白 - 凝乳酶系统之间存在的相似性。
