Spilberg I, Mehta J, Daughaday C, Simchowitz L
J Lab Clin Med. 1981 May;97(5):602-9.
3H-FMLP, a chemotactic peptide that resembles Escherichia coli chemotactic factor, is chemotactic for PAM, binds specifically to a site on the cell, and induces the generation of superoxide radicals by the cell. Scatchard analysis revealed an equilibrium dissociation constant at 26 degrees C of 1.45 x 10(-8)M and the presence of 1.7 , 10(5) receptors per cell. Binding was not inhibited by a partially purified C5a preparation or by the neutrophil-derived CCF but was inhibited by various N-formylated peptides. The order of potency of each peptide to inhibit 3H-FMLP binding was identical to the order of potency of each peptide to induce generation of superoxide by the PAM. Only small amounts of beta-glucuronidase activity and no lysozyme were detected in the supernatant after incubation of the cells for 30 min with varying concentrations of FMLP.
3H - FMLP是一种类似于大肠杆菌趋化因子的趋化肽，对多形核白细胞（PAM）具有趋化作用，能特异性结合细胞上的一个位点，并诱导细胞产生超氧自由基。Scatchard分析显示，在26摄氏度时平衡解离常数为1.45×10⁻⁸M，每个细胞存在1.7×10⁵个受体。部分纯化的C5a制剂或中性粒细胞衍生的趋化性细胞因子（CCF）不会抑制结合，但各种N - 甲酰化肽会抑制结合。每种肽抑制3H - FMLP结合的效力顺序与每种肽诱导PAM产生超氧的效力顺序相同。用不同浓度的FMLP孵育细胞30分钟后，上清液中仅检测到少量的β - 葡萄糖醛酸酶活性，未检测到溶菌酶。
