Subcellular distribution and properties of rabbit liver aminoacyl-tRNA synthetases under myocardial ischemia.

Subcellular distribution of aminoacyl-tRNA synthetase activities has been studied in normal rabbit liver and under experimental myocardial ischemia (EMI). An increase in the activity of a number of aminoacyl-tRNA synthetases in postmitochondrial and postribosomal supernatants from rabbit liver has been determined 12 hr after EMI. Gel chromatography of the postribosomal supernatant on Sepharose 6B shows that aminoacyl-tRNA synthetase activities are distributed among the fractions with M(r) 1.

[Interaction of eukaryotic aminoacyl-tRNA-synthases with polyribosomes].

Properties of rabbit liver tissue aminoacyl-tRNA synthetases, associated with polyribosomes, were studied under conditions of normal state and within 12 hrs after simulation of myocardium infarction. Under conditions of myocardium infarction the activity of some forms of aminoacyl-tRNA synthetase was decreased in polyribosomes and protein fractions, liberated from polyribosomes by means of washing with buffer containing 0.5 M KCl.

[Role of aminoacyl-tRNA-synthetases in changes in the rate of protein biosynthesis in the rabbit liver during myocardial ischemia].

Composition of high-molecular-weight aminoacyl-tRNA synthetases complexes from rabbit liver both in norm and after 12 h experimental myocardial ischemia (EMI) has been investigated. Partial redistribution of aminoacyl-tRNA synthetases activity from 1820 kD complex into 840 kD complex was observed in case of EMI which resulted in changes of protein biosynthesis rate in cell-free system.

[Distribution of aminoacyl-t-RNA-synthetase activity in rabbit liver cells during disruption of protein biosynthesis in experimental myocardia infarct].

Distribution of the aminoacyl-tRNA synthetase activity has been studied in the normal rabbit liver cells and in the model of protein synthesis damage, i.e. under experimental myocardial infarction (EMI).