Abstract
Three different gamma chains have been identified in fibrinogen isolated from normal human plasma with apparent molecular weights of 50000 (gamma 50), 55000 (gamma 55) and 57500 (gamma 57.5), as shown by SDS-polyacrylamide gel electrophoresis. Plasma fibrinogen was separated by ion-exchange chromatography on DEAE-Sephacel into three populations of molecules, each differing in gamma-chain composition. The first peak contained 87% of the total fibrinogen and was composed of molecules containing only gamma 50 chains; the second peak included 3% of the fibrinogen and contained one gamma 50 and one gamma 55 chain, and the third peak had 10% of the total which contained one gamma 50 and one gamma 57.5 chain. Cross-linked fibrin obtained from fibrinogen with only gamma 50 chains contained gamma gamma dimers exclusively of Mr 100000, representing a uniform gamma 50 gamma 50 dimer composition. The gamma gamma dimers from purified fibrinogen of gamma 50 gamma 55 type had molecular weights of 111000, 105000 and 100000, while dimers from gamma 50 gamma 57.5 fibrinogen were of Mr 115000, 108000 and 100000. The relative proportions of gamma gamma dimers from each purified fibrinogen population were consistent with random crosslinking of the ...Continue Reading
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