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Fibrin-fibrinogen interactions during gel filtration in a medium containing fibrinogen, albumin or cold-insoluble globulin

1981; Elsevier BV; Volume: 23; Issue: 1-2 Linguagem: Inglês

10.1016/0049-3848(81)90236-x

1879-2472

Wolfgang Krell, I. Mahn, N. Heimburger, G. Müller‐Berghaus,

Erythrocyte Function and Pathophysiology

In contrast to buffer, plasma can keep fibrin in solution at 20°C and at 37°C. In the present study the role played by fibrinogen, cold-insoluble globulin (CIg) and albumin in preventing fibrin precipitation was compared. Agarose gel filtration was performed using fibrinogen, CIg or albumin as an admixture to the equilibration and elution buffer. The addition of CIg or albumin to the equilibration and elution buffer did not significantly reduce the amount of des-AB fibrin precipitated on the columns. At 37°C, even more fibrin precipitated on the columns than at 20°C, when the elution buffer contained CIg, albumin or no protein admixture. In contrast to CIg and albumin, fibrinogen completely prevented precipitation of fibrin at 20°C as well as at 37°C, since about 100% of the fibrin applied to the columns were recovered in the effluent volume. When a mixture of 125I-des-AB fibrin and 131I-fibrinogen was chromatographed on these agarose columns, fibrin could be separated from fibrinogen. At 37°C, neither CIg nor albumin influenced fibrin-fibrinogen interactions. At 37°C, fibrin-fibrinogen complexes were not observed, possibly as gel filtration is not the adequate method for studying complex formation between fibrin and fibrinogen. The results suggest that fibrinogen is the main plasma protein in preventing fibrin precipitation at a physiologic ionic strength (0.15), a pH of 7.4 and a temperature of 37°C.