嗜中性粒细胞中性丝氨酸蛋白酶从血清免疫球蛋白G体外生成巨噬细胞趋化因子。
In vitro macrophage chemotactic generation from serum immunoglobulin G by neutrophil neutral seryl protease.
作者信息
Ishida M, Honda M, Hayashi H
出版信息
Immunology. 1978 Jul;35(1):167-76.
A neutral protease with a molecular weight of about 14,00 was separated at acid pH from rabbit neutrophils and then partially purified by elution on DEAE-Sephadex, CM-Sephadex and Sephadex G-75 in that order. This enzyme was inactivated by diisopropyl fluorophosphate (DFP), phenylmethyl sulphonylfluoride (PMSF), soybean trypsin inhibitor (SBTI), or elastatinal, suggesting a seryl protease resembling elastase, but it failed to digest elastin-orcein. The enzyme seemed different from histonase of rabbit neutrophils because of its haemoglobin (3HHb)-degrading ability and of inactivation by heparin. The protease generated in vitro macrophage chemotactic activity from guineapig serum IgG. This chemotactic factor had a molecular weight similar to that of IgG and its chemotacic generation was accompanied by release of dialysable peptide(s). No generation of macrophage chemotactic activity from IgG was induced in vitro by elastase from pig pancreas or by neutral thiol protease from rabbit neutrophils.
在酸性pH条件下从兔中性粒细胞中分离出一种分子量约为14,000的中性蛋白酶，然后依次通过DEAE-葡聚糖凝胶、CM-葡聚糖凝胶和葡聚糖凝胶G-75洗脱进行部分纯化。该酶被二异丙基氟磷酸酯（DFP）、苯甲基磺酰氟（PMSF）、大豆胰蛋白酶抑制剂（SBTI）或弹性蛋白酶抑制剂灭活，表明它是一种类似于弹性蛋白酶的丝氨酸蛋白酶，但它不能消化弹性蛋白-orcein。由于其降解血红蛋白（3HHb）的能力以及被肝素灭活，该酶似乎与兔中性粒细胞的组蛋白酶不同。该蛋白酶可从豚鼠血清IgG中体外产生巨噬细胞趋化活性。这种趋化因子的分子量与IgG相似，其趋化活性的产生伴随着可透析肽的释放。猪胰腺弹性蛋白酶或兔中性粒细胞中性巯基蛋白酶在体外均不能诱导IgG产生巨噬细胞趋化活性。
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