Literature DB >> 1191714

III. The RNA component of aminoacyl-tRNA synthetase complexes isolated from mouse liver. Absence of amino acid accepting activity.

B H Berg.   

Abstract

A method is described which permits the simultaneous isolation and separation of insoluble aminoacyl-tRNA synthetase protein - RNA complexes containing high specific synthetase activity, and soluble tRNA which retains 25% to 50% of its specific amino acid accepting activity. A possible amino acid accepting activity of the RNA part of the insoluble aminoacyl-tRNA synthetase protein - RNA complex was investigated by assaying the unchanged complex and the RNA obtained after dissociation from the protein part of the synthetase complex. No amino acid accepting activity was found.

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Year:  1975        PMID: 1191714     DOI: 10.1016/0005-2787(75)90212-9

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Phosphorylation of tRNA by T4 polynucleotide kinase.

Authors:  J R Lillehaug; K Kleppe
Journal:  Nucleic Acids Res       Date:  1977-02       Impact factor: 16.971

2.  Structural organization of high-Mr mammalian aminoacyl-tRNA synthetases. Comparison of multi-enzyme complexes from different sources.

Authors:  C V Dang; C V Dang
Journal:  Mol Cell Biochem       Date:  1984-09       Impact factor: 3.396

  2 in total

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