[alphaC domains of fibrinogen molecules as the structures accelerating fibrin assembly].

Preparation of monomeric fibrin lacking intact alpha C-domains (monomeric X1-fragment), but fully clottable, is described. The assembly process of both monomeric fibrin and monomeric X1-fragment has been studied by electron microscopy and light scattering methods. It was shown that both proteins form similar fibrils with characteristic cross-banding.

[Electron microscopic study of the DNA products of reverse transcription].

DNA-products synthesized on pre-mRNA's from rat liver and rabbit erythroidal bone marrow cells, on rabbit globin mRNA and the RNA-templates themselves have been examined by electron microscopy. In spreading conditions providing extension of molecules the sizes of DNA-products corresponded to sizes of RNA templates. Globin mRNA, pre-mRNA as well as cDNA synthesized on these templates in the presence of actinomycine D were seen as single-stranded molecules by electron microscopy.

[Electron microscopy study of fibrin self-assembly].

The process of fibrin selfassembly has been examined by electron microscopy. Its initial stage is found to consist in fibrin monomer conversion to thin filaments of random shape, probably identical with the well known intermediate polymers of fibrin. When the filaments attain an appropriate size they arrange themselfs into bundles with increasingly ordered structure.