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1
Aminoacylation of tRNA Trp from beef liver, yeast and E. coli by beef pancrease tryptophan-tRNA ligase. Stoichiometry of tRNATrp binding.
Nucleic Acids Res. 1977 Jan;4(1):31-42. doi: 10.1093/nar/4.1.31.
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Influence of magnesium on the steady-state-derived order of substrate addition and product release in tRNATrp aminoacylation by beef pancreas tryptophan: tRNA ligase: significance of the deduced mechanism.
Eur J Biochem. 1978 Jul 3;87(3):541-50. doi: 10.1111/j.1432-1033.1978.tb12405.x.
3
Kinetic evidence for half-of-the-sites reactivity in tRNATrp aminoacylation by tryptophanyl-tRNA synthetase from beef pancreas.
Biochemistry. 1986 Nov 4;25(22):7125-36. doi: 10.1021/bi00370a055.
4
Kinetic anticooperativity in pre-steady-state formation of tryptophanyl adenylate by tryptophanyl-tRNA synthetase from beef pancreas. A consequence of the tryptophan anticooperative binding.
Eur J Biochem. 1982 Nov 15;128(2-3):389-98. doi: 10.1111/j.1432-1033.1982.tb06977.x.
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Binding stoichiometry of tRNATrp and tryptophanyl-tRNA synthetase from bovine pancreas under pH conditions of maximum activity. Analysis by ultracentrifugation, fluorescence quenching and chemical modification.
Biochim Biophys Acta. 1987 Dec 18;916(3):350-7. doi: 10.1016/0167-4838(87)90180-4.
6
Position of aminoacylation of individual Escherichia coli and yeast tRNAs.
Proc Natl Acad Sci U S A. 1976 Feb;73(2):405-9. doi: 10.1073/pnas.73.2.405.
7
On the mechanism of tRNATrp aminoacylation catalysed by beef tryptophanyl-tRNA synthetase using presteady-state kinetics.
FEBS Lett. 1983 Jun 27;157(1):210-4. doi: 10.1016/0014-5793(83)81147-8.
8
Transfer RNA control of the activation of isomeric tRNATrp's.
J Biol Chem. 1979 Aug 10;254(15):6873-5.
9
The effect of tRNA and tryptophanyl adenylate on limited proteolysis of beef pancreas tryptophanyl-tRNA synthetase.
Nucleic Acids Res. 1979 Oct 10;7(3):625-37. doi: 10.1093/nar/7.3.625.
10
Negative cooperativity in adenylate formation catalysed by beef pancreas tryptophanyl-tRNA synthetase: influence of tRNATrp.
FEBS Lett. 1982 Jan 11;137(1):95-9. doi: 10.1016/0014-5793(82)80322-0.
引用本文的文献
1
Study of the interactions between avian myeloblastosis virus reverse transcriptase and primer tRNA. Affinity labeling and inactivation of the enzyme by periodate-treated tRNATrp.
Nucleic Acids Res. 1980 Sep 11;8(17):4009-20. doi: 10.1093/nar/8.17.4009.
本文引用的文献
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AMINO ACID ACCEPTOR ACTIVITY OF ENZYMICALLY ALTERED SOLUBLE RNA FROM ESCHERICHIA COLI.
Biochim Biophys Acta. 1964 Apr 27;80:574-86. doi: 10.1016/0926-6550(64)90302-0.
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Measurement of protein-binding phenomena by gel filtration.
Biochim Biophys Acta. 1962 Oct 8;63:530-2. doi: 10.1016/0006-3002(62)90124-5.
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Beef pancreas tryptophanyl-tRNA synthetase. Molecular weight, composition and spectral properties.
Eur J Biochem. 1969 Sep;10(2):336-44. doi: 10.1111/j.1432-1033.1969.tb00695.x.
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[Purification of tryptophan tRNA synthetase from beef pancreas].
Bull Soc Chim Biol (Paris). 1969 Jul 25;51(3):495-510.
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The subunit structure of tryptophanyl transfer ribonucleic acid synthetase from beef pancreas.
J Biol Chem. 1972 May 10;247(9):2931-43.
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Purification of methionine-, valine-, phenylalanine- and tyrosine-specific tRNA from Escherichia coli.
Biochim Biophys Acta. 1967 Jun 20;142(1):133-48. doi: 10.1016/0005-2787(67)90522-9.
8
Structure-activity relationship in tryptophanyl-transfer ribonucleic acid synthetase from beef pancreas. Role of -SH groups in the activity of the enzyme.
Eur J Biochem. 1973 Nov 15;39(2):547-56. doi: 10.1111/j.1432-1033.1973.tb03153.x.
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Tryptophanyl-transfer ribonucleic-acid synthetase from beef pancreas. Ligand binding and dissociation equilibrium between the active dimeric and inactive monomeric structures.
Eur J Biochem. 1973 Nov 1;39(1):275-82. doi: 10.1111/j.1432-1033.1973.tb03124.x.
10
Kinetics of homologous and heterologous aminoacylation with yeast phenylalanyl transfer ribonucleic acid synthetase.
Biochemistry. 1973 Oct 9;12(21):4146-54. doi: 10.1021/bi00745a018.
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