Fractionation and specificities of two aspartyl-ribonucleic acid and two phenylalanyl-ribonucleic acid synthetases.
نویسندگان
چکیده
منابع مشابه
The Aminoacyl Ribonucleic Acid Synthetases
Threonyl ribonucleic acid synthetase was purified 400-fold from rat liver. During stepwise chromatography on diethylaminoethyl cellulose, two fractions with this enzymatic activity were observed. The separated fractions give distinct elution patterns on rechromatography on the same ion exchanger. Threonyladenylate-enzyme complex prepared with 14Cthreonine and 3H-adenosine triphosphate shows a s...
متن کاملSpecies Specificity of Amino Acid Acceptor Ribonucleic Acid and Aminoacyl Soluble Ribonucleic Acid Synthetases.
Several investigators have reported that the activation of amino acids for protein synthesis, i.e. the incorporation of amino acids into soluble ribonucleic acids, is dependent upon the source of both the aminoacyl S-RNA’ synthetases and the S-RNA itself. For example, Rendi and Ochoa (1) reported that aminoacyl S-RNA synthetases from Escherichia coli could not incorporate leucine into yeast or ...
متن کاملAffinity chromatography of aminoacyl-transfer ribonucleic acid synthetases. Cognate transfer ribonucleic acid as a ligand.
The use of tRNA affinity columns for the purification of aminoacyl-tRNA synthetases was investigated. A purification method for valyl-tRNA synthetase from Bacillus stearothermophilus is described that uses two affinity columns, one containing the pure cognate tRNA, and the other containing all tRNA species except the cognate tRNA. A method for the rapid preparation of the two columns was develo...
متن کاملInteractions of Phenylalanyl Transfer Ribonucleic Acid Synthetase of Neurospora crassa with Valyl Transfer Ribonucleic Acid of Escherichia co&*
Since Phe-tRNA synthetase of Neurospora crassa reacts with tRNAV”’ of Escherichia coli to produce Phe-tRNAV&‘, the parameters that effect the reverse reaction were examined. Similarly, the interaction of Val-tRNA synthetase (E. coti) with Phe-tRNAVal and Val-tRNAVal (E. coli) was studied. Phe-tRNA synthetase (N. crassa) can catalyze the deacylation of both Phe-tRNAVa 1 (E. coli) and Val-tRNAV”’...
متن کاملInteractions of phenylalanyl transfer ribonucleic acid synthetase of Neurospora crassa with valyl transfer ribonucleic acid of Escherichia coli.
Since Phe-tRNA synthetase of Neurospora crassa reacts with tRNAV”’ of Escherichia coli to produce Phe-tRNAV&‘, the parameters that effect the reverse reaction were examined. Similarly, the interaction of Val-tRNA synthetase (E. coti) with Phe-tRNAVal and Val-tRNAVal (E. coli) was studied. Phe-tRNA synthetase (N. crassa) can catalyze the deacylation of both Phe-tRNAVa 1 (E. coli) and Val-tRNAV”’...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1966
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.55.1.184