Turbidity development registration and electron microscopic observation of the assembly process of the fibrin monomer and its derivative lacking in intact αC‐domains (monomeric X1 fragment) have shown that these domains participate in fibrin polymerization, not as structural components, but as a factor promoting the ordered process of fibrin assembly.
SUMMARYThe structure of the iridescent virus type I was examined using negative staining technique. After storage for r to z months at 4 °C or treatment with chloroform, the icosahedral capsid breaks up into its structural elements-pentagons and triangles, each consisting of 31 and 55 subunits respectively. When such a preparation is centrifuged through a linear sucrose gradient (Io to 4o%), 5 zones are revealed. An electron microscopic analysis showed the following distribution of the material (from top to bottom of the tube): (i) free triangles; (z) associated triangles, 'core'; (3) partially disrupted virions; (4) free intact virus particles; (5) virus aggregates.A model for iridescent virus type I capsid is proposed, consisting of I2 pentagons (372 subunits) and 20 triangles (I IOO subunits). The total number of subunits is I472.
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