ヒトフィブリン寒天平板(H-FAP)法による線溶活性測定について

抄録

Human fibrin-agar plate (H-FAP) method for the estimation of fibrinolytic activity is described. This method using human fibrinogen is based on the Fibrin-Agar-Plate (FAP) method reported previously (3).
Human fibrinogen was purified by removal of plasminogen and plasmin directly from the commercial fibrinogen by affinity chromatography (Cuatrecasas et al. (4) and Mertz et al. (6)). Four protein bands were separated by disc electrophoresis from the purified fibrinogen obtained as above. No lysis was observed in the presence of urokinase or streptokinase over the range of units tested, when fibrinogen has been clotted with thrombin. This was also confirmed in thrombelastogram.
The H-FAP was prepared in a similar manner as described in the previous report (3): Seven ml of a barbital buffer solution containing 2% of agar (pH 7.8) were mixed with 3 ml of the same buffer solution containing 3 mg of purified human fibrinogen at 40 to 50°C. When the agar-fibrinogen mixture has solidified as gel at room temperature, 5 units (1.5 ml) of thrombin were added. Twenty units of U. K. were found optimal for the activation of euglobulin.
Various samples can be compared and observed for a long period in diseases related to fibrinolysis in the same lot of H-FAP, because it is stable when stored in a refrigerator (4°C).