The Fibrinogen Molecule: Its Size, Shape, and Mode of Polymerization

doi:10.1083/jcb.5.1.11

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ARTICLE

The Fibrinogen Molecule: Its Size, Shape, and Mode of Polymerization

Cecil E. Hall Ph.D.¹ and Henry S. Slayter ¹

¹ From the Department of Biology, Massachusetts Institute of Technology, Cambridge

Improved electron micrographs of the shadow-cast bovine fibrinogenmolecule have been obtained establishing its general morphologyand dimensions in the dry state. It consists of a linear arrayof 3 nodules held together by a very thin thread which is estimatedto have a diameter of from 8 to 15 A, though it is not clearlyresolved. The two end nodules are alike but the center one isslightly smaller. Measurements of shadow lengths indicate thatnodule diameters are in the range 50 to 70 A. The length ofthe dried molecule is 475 ± 25 A.

Adopting the molecularvolume from previous physical chemical data and the generalmorphological features and length from electron microscopy,we calculate the diameters of the end nodules to be 65 A andthe center one as 50 A. The model of the molecule so obtainedis consistent with the electron microscopical observations andthe data from physical chemistry.

The intermediate polymersformed when fibrinogen is activated with thrombin were alsoexamined and found to be end-to-end aggregates of altered fibrinogenmolecules which shrink in length during the process. Intermediatepolymer lengths are from 1000 to 5000 A.

The nodular natureof fibrinogen, its shrinkage and end-to-end aggregation on polymerizationpermits us to deduce an explanation for the system of cross-bandspreviously observed in stained fibrin fibrils.

Submitted on August 18, 1958

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