Thrombin-catalyzed fibrin polymerization 試験によるフィブリノゲン機能解析

概要

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We studied the functional deviation of three dysfibrinogens (A, B and C) from the normal with thrombin-catalyzed fibrin polymerization (TCFP). The test condition of the TCFP, however, has not yet been standardized in spite of its striking dependency on pH, ionic strength and concentrations of Ca ion and of fibrinogen. This led us to establish the optimal condition, using purified normal plasma fibrinogen. The result obtained was as follows : 0.05 M triethanolamine-HCl buffer of pH 7.4 with 0.1 M NaCl and without Ca ion at the beginning. The test was best appreciable at 0.25 mg/ml of fibrinogen, since the 'velocity' and 'amplitude' showed a proportional linearity to the concentration, unless beyond the point. On the condition described above, the A and C dysfibrinogens demonstrated remarkable elongation of lag time and significant decrease in velocity and amplitude in comparison with normal control. The B, on the other hand, revealed much smaller deviation, which improved to almost normal by addition of Ca ion (5 mM) of the system. Interestingly, the abnormal amino acids are situated near the Ca binding site of gamma chain in B dysfibrinogen, while they are far from it in the A and C.
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