[Protein synthesis and content of free amino acids in rat organs in experimental peritonitis].

Experiments performed on rats shown that in peritonitis the mass of the animal's organs and C14-amino acid incorporation into tissue proteins is reduced. Free amino acid content in tissues and serum is increased. Decreased incorporation of C14-amino acid into hepatic proteins antecedes the increase of free amino acid content in this organ.

[Biosynthesis of proteins in various organs of albino rats in experimental peritonitis].

Protein biosynthesis and the state of polysomes were studied in rat liver and spleen tissues under conditions of acute purulent peritonitis of abdominal cavity. In the both tissues studied synthesis of proteins was markedly inhibited at the initial period of the peritonitis development within 6 hrs, these patterns were further increased within 12-48 hrs but they remained lower the control values. The structure-functional impairments of polysomes were most distinct within 24-48 hrs after the disease beginning.

[RNA biosynthesis in various organs of the rat in experimental peritonitis].

Synthesis of various RNA species was studied in liver, spleen, and kidney tissues of one year old Wistar rat males within 6, 12, 24 and 48 hrs after peritonitis development. RNA biosynthesis was found to be unaltered in kidney; in liver tissue it was distinctly decreased beginning from 24 hrs and lowered down to 40% of the control value within 2 days. In spleen an increase in synthesis of pro-mRNA (90%) and mRNA was observed at early steps of peritonitis, with the subsequent decrease of these patterns within 24-48 hrs as compared with the previous periods of the disease as well as with controls.

[Nuclear RNP containing pre-mRNA. 16. Cross-linked informofers].

The proteins of 30S RNP particles containing pre-mRNA (hnRNA) were cross-linked with bifunctional reagents (dimethylsuberimidate and dimethyl-3,3'dithiobispropionimi-date). Further treatment with 1 or 2 M NaCl dissociates all RNA from protein. However, a significant part of protein particles--informofers, being cross-linked survived high salt treatment.

Cross-linked informofers.

The proteins of 30S RNP particles containing pre-mRNA (hnRNA) were cross-linked with bifunctional reagents (dimethyl-suberimidate and dimethyl-3,3'-dithiobispropionimidate). Further treatment with 1 or 2 M NaCl dissociates all RNA from protein. However, a significant part of protein particles--informofers being cross-linked survived high salt treatment.

[Nuclear ribonucleoproteins containing pro-mRNA. XIV. Structural study using ethidium and fluorescamine].

Nuclear 30S RNP particles were studied by means of fluorescence techniques. It's shown that fluorescamin interacts with NH2-groups of protein molecule. As a result, covalent fluorescent label is formed.

[Nuclear RNP, containing pre-mRNA. XIV. Nature of particles, containing 5'- and 3'-end structures].

Some characteristic peculiarities of the 5'-end and 3'-end structures of pre-mRNA isolated from nuclear RNP particles have been investigated: presence of triphosphorylated nucleotides on the 5'-ends, as a characteristic of the primary product of transcription; presence of modified 5'-ends -- blocked and methylated structures -- caps; presence of poly(A) blocks attached to the 3'-end of pre-mRNA during post-transcriptional transformation of the latter. It was shown that pre-mRNA isolated from nuclear RNP particles contained triphosphorylated nucleotides as well as a "cap" structure at the 5'-ends. On the 3'-ends of pre-mRNA from nuclear RNP particles isolated in the presence of a RNAse inhibitor, the presence of poly(A) blocks have been shown.