Herion J C, Bucher J R, Penniall R, Walker R I, Baker M, Roberts H R
Am J Hematol. 1979;7(3):265-79. doi: 10.1002/ajh.2830070309.
Lysosomes (granules) of rabbit PMN leukocytes were extracted with either HCl or H2SO4, and the extracts were chromatographed over Sephadex to separate protein constituents. Some of the low molecular weight cationic proteins homogeneous on SDS PAGE (8% and 12.5% gels) were characterized by electrophoretic mobility in acid gels and by amino acid analysis. A 3,700 dalton polypeptide, rich in arginine and cysteine, prolonged the partial thromboplastin time of normal plasma. In low concentration, this protein shortened the clotting time of pure fibrinogen by thrombin. In high concentration this lysosomal cationic protein precipitated fibrinogen from solution; no fibrinopeptides were released to suggest cleavage of fibrinogen. Fibrinolytic protease activity was detected in crude H2SO4 extracts but not in crude HCl extracts. Two separate plasminogen activators, differing from kallikrein or prekallikrein, were isolated from the H2SO4 lysosomal extract and were partially characterized; neither exhibited proteolytic activity on fibrinogen free of plasminogen.
用盐酸或硫酸提取兔中性粒细胞的溶酶体（颗粒），提取物经葡聚糖凝胶柱层析以分离蛋白质成分。一些在SDS-PAGE（8%和12.5%凝胶）上呈均一性的低分子量阳离子蛋白，通过酸性凝胶中的电泳迁移率和氨基酸分析进行了表征。一种富含精氨酸和半胱氨酸的3700道尔顿多肽，延长了正常血浆的部分凝血活酶时间。在低浓度下，这种蛋白质可缩短凝血酶作用下纯纤维蛋白原的凝血时间。在高浓度下，这种溶酶体阳离子蛋白可使纤维蛋白原从溶液中沉淀出来；未释放出纤维蛋白肽，提示纤维蛋白原未被裂解。在硫酸粗提物中检测到纤溶蛋白酶活性，但在盐酸粗提物中未检测到。从硫酸溶酶体提取物中分离出两种不同于激肽释放酶或前激肽释放酶的纤溶酶原激活剂，并对其进行了部分表征；两者对不含纤溶酶原的纤维蛋白原均无蛋白水解活性。
