Abstract
The fine structure of polymers resulting from the action of thrombin and protamine sulfate on three specimens of purified human fibrinogen was studied with the electron microscope. The basic pattern of both polymers, “protamine sulfate-fibrin” and “thrombin-fibrin”, was very similar. The average periodicity of thrombin-fibrin was 239 Å in shadowed and 228 Å in negatively-stained preparations. The average periodicity of protamine sulfate-fibrin was 225 Å in shadowed and 223 Å in stained preparations. The network of protamine sulfate-fibrin formed from one specimen of fibrinogen (Cutter, Calif.) was extensive and exhibited branching typical of that observed in thrombin-induced clots from all specimens of fibrinogen. The networks of protamine sulfate-fibrin formed from two other specimens of fibrinogen (Kabi, Sweden and Jamieson, Washington, D.C.) were limited and were composed of short, broad strands with bluntly tapered ends. It is postulated that protamine sulfate brings about nonenzymatic polymerization of fibrinogen by neutralizing the negative charge on fibrinopeptides.
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