Edmonds S, Gibb A, Sim E
Department of Pharmacology, University of Oxford, U.K.
Biochem J. 1993 Feb 1;289 ( Pt 3)(Pt 3):801-5. doi: 10.1042/bj2890801.
Thiol compounds have been investigated as inhibitors of the covalent binding reaction of human complement protein C4 using Sepharose-C1s as a combined activating and binding surface. o- and p-substituted aminothiophenols are equally effective inhibitors, whereas the m-substituted compound is a less potent inhibitor. The anti-hypertensive drug captopril is also shown to inhibit the covalent binding reaction. A comparison of the effects of these compounds on the covalent binding reaction of isolated C4A and C4B has been made. Results suggest that a Pro-to-Leu substitution in C4B is likely to account for the differences in inhibitory potency of C4B compared with C4A observed with the aromatic inhibitors.
已使用琼脂糖-C1s作为联合激活和结合表面,研究了硫醇化合物作为人补体蛋白C4共价结合反应抑制剂的情况。邻位和对位取代的氨基硫酚是同样有效的抑制剂,而间位取代的化合物是效力较弱的抑制剂。抗高血压药物卡托普利也显示出能抑制共价结合反应。已对这些化合物对分离的C4A和C4B共价结合反应的影响进行了比较。结果表明,C4B中脯氨酸到亮氨酸的取代可能是造成与芳香族抑制剂观察到的C4A相比C4B抑制效力差异的原因。