Fibrin assembly: a comparison of electron microscopic and light scattering results.
To test the validity of a proposed two step fibrin assembly mechanism and directly visualize the molecular species present at various stages of fibrin formation, we have carried out an electron microscopic investigation. Assembly conditions duplicated those of a recent light scattering study and specimens were prepared at different time points with the use of a negative staining technique recently employed to visualize the trinodular structure of fibrinogen. Under near-physiological buffer conditions, protofibrils structurally similar to those postulated by Ferry have been found at early stages of fibrin assembly. In parallel with the light scattering results, a dramatic increase in fiber diameter was found in specimens prepared during the postulated lateral association stage of gelation. Light scattering and electron microscopic results both showed that high ionic strength reduces the rate and extent of fiber formation. Reptilase cleavage is shown to result in typical cross striated fibrin.
D012103:Batroxobin; D005337:Fibrin / Q000032:analysis* / Q000096:biosynthesis; D005340:Fibrinogen / Q000032:analysis; D006801:Humans; D008027:Light; D008854:Microscopy, Electron; D008968:Molecular Conformation; D012542:Scattering, Radiation; D013194:Staining and Labeling; D013917:Thrombin
D005337:Fibrin; D005340:Fibrinogen; D012103:Batroxobin; D013917:Thrombin