Malemud C J, Janoff A
Arthritis Rheum. 1975 Jul-Aug;18(4):361-8. doi: 10.1002/art.1780180413.
Human polymorphonuclear neutrophil (PMN) granule extract (25 mug of protein) released 60 percent of the available 35SO4 from labeled rabbit articular cartilage in 0.5 hour at neutral pH. N-acetyl-L-alanyl-L-alanyl-L-prolyl-L-alanine choloromethyl ketone (NAcAAPACK), a specific elastase inhibitor, was only minimally effective against whole granule extract, and N-alpha-tosyl-L-lysine chloromethyl ketone, which inhibits trypsin but not elastase, was completely ineffective. Preparative disc-gel electrophoresis of PMN granule extract revealed two separate regions with independent activity against 35SO4-labeled cartilage. One region contained elastases and when tested alone, was completely inhibited by NAcAAPACK. The other contained lysozyme and two esterases active against N-acetyl-L-phenylalanine-alpha-naphthol. Purified lysozyme proved inactive, suggesting that the chymotrypsin-like esterases were responsible for proteoglycan degradation by this region of the gel.
人多形核中性粒细胞（PMN）颗粒提取物（25微克蛋白质）在中性pH值下，0.5小时内从标记的兔关节软骨中释放出60%的可用35SO4。N-乙酰-L-丙氨酰-L-丙氨酰-L-脯氨酰-L-丙氨酸氯甲基酮（NAcAAPACK）是一种特异性弹性蛋白酶抑制剂，对整个颗粒提取物的作用极小，而抑制胰蛋白酶但不抑制弹性蛋白酶的N-α-甲苯磺酰-L-赖氨酸氯甲基酮则完全无效。PMN颗粒提取物的制备性圆盘凝胶电泳显示出两个独立的区域，它们对35SO4标记的软骨具有独立活性。一个区域含有弹性蛋白酶，单独测试时，完全被NAcAAPACK抑制。另一个区域含有溶菌酶和两种对N-乙酰-L-苯丙氨酸-α-萘酚有活性的酯酶。纯化的溶菌酶证明无活性，这表明类胰凝乳蛋白酶酯酶是该凝胶区域蛋白聚糖降解的原因。
