{'fraction_non_alphanumeric': 0.05309734513274336, 'fraction_numerical': 0.02654867256637168, 'mean_word_length': 5.058035714285714, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
[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). The activity of a number of aminoacyl-tRNA synthetases in postmitochondrial and postribosomal extracts from rabbit liver homogenate has been determined to increase 12 h after EMI. Gel filtration of the postribosomal extract on Sepharose 6B shows that the activity of aminoacyl-tRNA synthetases is distributed among the fractions with Mr 1.82 x 10(6), 0.84 x 10(6) and 0.12 = 0.35 x 10(6). The first two fractions (high-molecular-weight aminoacyl-tRNA synthetase complexes) contain arginyl-, glutamyl-, isoleucyl-, leucyl-, lysyl- and valyl-tRNA synthetases, whereas the low-molecular-weight fraction contains alanyl-, arginyl-, glycyl-, phenylalanyl-, seryl-, threonyl-, tryptophanyl- and tyrosyl-tRNA synthetases. In a case of EMI all the aminoacyl-tRNA synthetases translocate from the complexes with Mr 1.82 x 10(6) into the complexes with Mr 0.84 x 10(6), what provided evidence for the possibility to regulate protein synthesis by changes in compartmentalization of aminoacyl-tRNA synthetases.