Modification of Escherichia coli Glutamate Transfer Ribonucleic Acid with Bisulfite
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چکیده
منابع مشابه
Viral modification of the valyl transfer ribonucleic acid synthetase of Escherichia coli.
The valyl-tRNA synthetase (EC 6.1.1.9) of Escherichia coli was compared to the modified form of the enzyme which develops during infection by bacteriophage T4. The two forms were found to differ in their stability to heat, stability to urea, ability to charge yeast tRNA, electrophoretic mobility, sedimentation rate in sucrose gradients, and molecular size. Both enzyme activities are easily puri...
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Escherichia coli glutamyl transfer ribonucleic acid synthetase acylates the three homologous tRNAGIU isoacceptors with very similar K, values (2.4 to 4.6 X lop7 M). The pure enzyme forms a 1: 1 complex with its cognate tRNA as judged by gradient centrifugation and fluorescence-quenching studies. The biological specificity of complex formation is not strictly observed in vitro since fluorescence...
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Escherichia coli strain NP2907 was isolated as a spontaneous mutant of strain NP29, which possesses a thermolabile valyl-transfer ribonucleic acid (tRNA) synthetase. The valyl-tRNA synthetase of the new mutant, unlike that of its immediate parent, retains enzymatic activity in vitro but differs from the wild-type enzyme in stability and apparent K(m) for adenosine triphosphate. The new mutant l...
متن کاملThe arginyl transfer ribonucleic acid synthetase of Escherichia coli.
The arginyl transfer ribonucleic acid (tRNA) synthetase of Escherichia coli has been purified over SO&fold. Its kinetic properties are similar to those of other amino acidactivating enzymes; it has a pH optimum near 8 and does not react with amino acids that occur in proteins other than arginine, but the analogues homoarginine and canavanine are competitive inhibitors, and canavanine can be est...
متن کاملGlutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli
Escherichia coli glutamyl transfer ribonucleic acid synthetase acylates the three homologous tRNAGIU isoacceptors with very similar K, values (2.4 to 4.6 X lop7 M). The pure enzyme forms a 1: 1 complex with its cognate tRNA as judged by gradient centrifugation and fluorescence-quenching studies. The biological specificity of complex formation is not strictly observed in vitro since fluorescence...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)61887-3