Braun N J, Schnebli H P
Biol Chem Hoppe Seyler. 1987 Feb;368(2):155-61. doi: 10.1515/bchm3.1987.368.1.155.
The interaction of Eglin c with human polymorphonuclear cells was investigated in order to explain the effect of this (and other) proteinase inhibitor(s) on the biological activities of neutrophils. We have identified binding sites on human neutrophils by using [3H]Eglin. Binding is rapid and reversible at 5 degrees C. There are approximately 100,000 binding sites per cell, with an equilibrium dissociation constant of 0.2microM. Eglin binding was not inhibited by other proteinase inhibitors (alpha 1-PI, PhCH2SO2F, Tos-Phe-CH2Cl), and was enhanced four-fold by the chemotactic peptide fMet-Leu-Phe. The results indicate that Eglin c, a peptide proteinase inhibitor, is able to bind to human PMN cells and that this initial interaction does not involve a known proteinase such as cathepsin G or elastase.
为了解释这种（及其他）蛋白酶抑制剂对中性粒细胞生物学活性的影响，对埃格林c与人多形核细胞的相互作用进行了研究。我们通过使用[3H]埃格林确定了人中性粒细胞上的结合位点。在5℃下，结合迅速且可逆。每个细胞约有100,000个结合位点，平衡解离常数为0.2μM。埃格林的结合不受其他蛋白酶抑制剂（α1-抗胰蛋白酶、苯甲基磺酰氟、甲苯磺酰苯丙氨酰氯甲基酮）的抑制，而趋化肽甲酰甲硫氨酰-亮氨酰-苯丙氨酸可使其结合增强四倍。结果表明，肽类蛋白酶抑制剂埃格林c能够与人中性粒细胞结合，且这种初始相互作用不涉及组织蛋白酶G或弹性蛋白酶等已知蛋白酶。
