フィブリン構造と系の濁度に関する研究 （ＩＩ）

Abstract

In the fibrinogen-fibrin conversion, remarkable turbidity changes can be observed in experimental conditions of both a neutral pH and low ionic strength. The relationships between fibrin structure and turbidity changes were studied. In the region, which slope is designated as αI, of the initial small turbidity changes on the turbidity-time curve obtained experimentally, the hydrolysis of fibrinogen by thrombin was stopped by adding a potent thrombin inhibitor MD-805. Then dimer and trimer of fibrin monomers, detected from the reaction mixture by a SDS (0.1%)-agarose (2%) gel electrophoresis, were regarded as nuclei of polymerization of fibrin monomers.On the other hand, the region, which slope is designated as αII, of the most remarkable turbidity change, e. g., αII/αI=10, on the turbidity-time curve could be attained neither by increase of the equilibrium constants in the simplified model for the polymerization of fibrin monomer nor by the formation of infinitely long fibrin polymer. Thus, the remarkable turbidity changes in the fibrinogen-fibrin conversion was deduced not only by the contribution of the growth of protofibrils but also by the lateral association of protofibrils.