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H Brzuszkiewicz-Zarnowska

Publications and source records attributed to H Brzuszkiewicz-Zarnowska.

8 recordsLinked to original sources

Mitochondrial tRNA in hyperthyroidism.

The mitochondrial tRNA were prepared from liver and brain tissues of thyroxinized and control rabbits. The presence of tRNA for twenty amino acids both in liver and brain mitochondria was revealed. The quantity of radioactive amino acids bound to the mitochondrial tRNA was higher in hyperthyreosis than in control animals but considerable differences between the brain and liver tissues were observed.

Animals↗

Activity of aminoacyl-tRNA synthetases in experimental hyperthyroidism in muscle tissues of the rabbit.

In cardial and femoral muscles of rabbits specific activities of aminoacyl-tRNA synthetases for twenty amino acids were generally similar, namely the activities towards amino acids and their amides, leucine, isoleucine, histidine, tyrosine, proline and serine were considerably lower than towards the remaining amino acids. Specific activities of most aminoacyl-tRNA synthetases were higher in hyperthyroidism than in euthyreosis, and were higher in femoral muscle than in heart. The response to thyroxine treatment of individual aminoacyl-tRNA synthetases in both kinds of muscles varied with respect to most of the amino acids.

Amino Acyl-tRNA Synthetases↗

[Tissue levels of some elements in hyperthyreosis in rabbits].

The aim of the present study was to estimate the concentration of Cu, Zn, Mg, Ca in the following tissues: brain, heart, lung, liver, kidney and femoral muscles in conditions of experimentally induced hyperthyreosis. In general, in state of hyperthyreosis the concentration of all elements was considerably higher compared to euthyreosis. However, there are a few exceptions. Liver and heart tissue possessed higher concentration of Zn and Cu and kidney of Cu in euthyreosis.

Animals↗

Isolation from calf brain of a polypeptide fraction affecting aminoacylation of tRNA.

The preparation of tRNA obtained from calf brain by three conventional methods exhibits the presence of a slow-migrating fraction in polyacrylamide-gel electrophoresis. This fraction constitutes 2-2.5% of the isolated tRNA and has been identified as a polypeptide of molecular weight of 6000. The aminoacylation with glutamic acid, glycine, leucine and phenylalanine of tRNA devoid of this polypeptide is reduced by half as compared with the initial preparation.

Amino Acyl-tRNA Synthetases↗