Wilson P A
J Clin Pathol. 1968 Mar;21(2):147-53. doi: 10.1136/jcp.21.2.147.
The digestion of fibrinogen with various concentrations of trypsin results in the formation of a variety of degradation products. Degradation products formed in this way have been purified by DEAE cellulose column chromatography and their effects on platelet aggregation investigated.TWO METHODS HAVE BEEN USED TO STUDY PLATELET AGGREGATION: a turbidimetric method which assesses platelet aggregation by the ability of adenosine diphosphate (ADP) to clump platelets and a method which assesses platelet adhesiveness by their ability to adhere to glass and to each other (modified Hellem technique, 1960). Three breakdown products produced by trypsin-digested fibrinogen were studied and all showed ;antithrombin' activity: two inhibited platelet aggregation, but one accelerated aggregation in both systems. Another product prepared by digestion of fibrinogen with urokinase-activated plasminogen has been shown to possess the ability to enhance ADP-induced platelet aggregation.
用不同浓度的胰蛋白酶消化纤维蛋白原会产生多种降解产物。以这种方式形成的降解产物已通过二乙氨基乙基纤维素柱色谱法进行纯化，并研究了它们对血小板聚集的影响。研究血小板聚集采用了两种方法：一种比浊法，通过二磷酸腺苷（ADP）使血小板聚集的能力来评估血小板聚集；另一种方法是通过血小板粘附于玻璃以及相互粘附的能力来评估血小板粘附性（改良的赫勒姆技术，1960年）。研究了胰蛋白酶消化纤维蛋白原产生的三种分解产物，它们均表现出“抗凝血酶”活性：其中两种抑制血小板聚集，但有一种在两种系统中均加速聚集。已证明，用尿激酶激活的纤溶酶原消化纤维蛋白原制备的另一种产物具有增强ADP诱导的血小板聚集的能力。
