Comparison of the enzymatic behavior of high molecular weight and free lysyl-tRNA synthetase from rat liver: kinetic analysis of lysylation of tRNA

Wahab, Samir Z.; Yang, David C.H.

doi:10.1016/0003-9861(86)90017-2

Cited by 6 publications

(4 citation statements)

References 30 publications

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“…The materials and the general analytical methods have been described (Wahab & Yang, 1986). Buffer T contained 20 mM Tris-HCl1 (pH 7.2), 2 mM DTE, 3 mM MgCl2, and 10% glycerol.…”

Section: Methodsmentioning

confidence: 99%

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Purification of mammalian histidyl-tRNA synthetase and its interaction with myositis-specific anti-Jo-1 antibodies

Fahoum¹,

Yang²

1987

Biochemistry

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“…The materials and the general analytical methods have been described (Wahab & Yang, 1986). Buffer T contained 20 mM Tris-HCl1 (pH 7.2), 2 mM DTE, 3 mM MgCl2, and 10% glycerol.…”

Section: Methodsmentioning

confidence: 99%

“…Inhibition Patterns by Anti-Jo-1 IgG The initial velocity of aminoacylation was determined for each substrate by varying its concentration while the other two substrates were kept at saturating concentrations as described previously (Wahab & Yang, 1986). This was carried out in the absence or presence of purified anti-Jo-1 IgG.…”

Section: Hydrodynamic Parametersmentioning

confidence: 99%

Purification of mammalian histidyl-tRNA synthetase and its interaction with myositis-specific anti-Jo-1 antibodies

Fahoum¹,

Yang²

1987

Biochemistry

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“…The concentration of RNA was determined from the absorbance at 260 nm. Aminoacyl-tRNA synthetase activities were assayed by measuring the rate of aminoacylation of tRNA as previously described (Wahab & Yang, 1986) except using the following reaction mixture (in 50-/iL aliquots): 50 mM Tris-HCl (pH 7.5) , 3 mM MgCl2, 2 mM DTE, 2.0 mM ATP, 0.05 mM 14C-labeled amino acid (50-300 mCi/mmol), 2 mg/mL BSA, and 5 mg/mL tRNA.…”

Section: Methodsmentioning

confidence: 99%

Structural organization of the multienzyme complex of mammalian aminoacyl-tRNA synthetases

Godar

Garcia²,

Jacobo³

et al. 1988

Biochemistry

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The multienzyme complexes of mammalian aminoacyl-tRNA synthetases were purified from rat liver, rabbit liver, and rabbit reticulocytes according to the procedure slightly modified from Kellermann et al. [Kellermann, O., Brevet, A., Tonetti, H., & Waller, J.-P. (1979) Eur. J. Biochem. 99, 541-550]. Three forms of the synthetase complex with slightly different protein compositions were identified, suggesting a microheterogeneity of the synthetase complex. The hydrodynamic properties and the protein composition of the purified complexes were determined. The electron micrographs of the complex showed mostly amorphous particles and some hollow rings with an outer diameter of 164 A and an inner diameter of 42 A. The predicted hydrodynamic properties of several models of the complex were calculated. The properties of a ring model appear to best fit with those of the synthetase complex.

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“…The materials and the general methods have been described (Wahab & Yang, 1986). Buffer T contained 50 mM tris-(hydroxymethyl)aminomethane hydrochloride (Tris-HCl) (pH 7.5 at 25 °C), 4 mM MgCl2, 2 mM dithioerythritol (DTE), 10% glycerol, 0.04% NaN3, and 0.5 mM phenylmethanesulfonyl fluoride (PMSF) which was added immediately before use from a 200 mM stock solution in isopropyl alcohol.…”

Section: Methodsmentioning

confidence: 99%

Mammalian high-molecular-weight and monomeric forms of valyl-tRNA synthetase

Godar

Yang²

1988

Biochemistry

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Valyl-tRNA synthetase from rat liver sediments at 15.5 S with a Stokes radius of 90 A, corresponding to a native molecular weight of 585,000. Purification of valyl-tRNA synthetase to homogeneity by a combination of conventional and affinity column chromatography yields a fully active monomeric form of valyl-tRNA synthetase with a sedimentation coefficient of 7.7 S and a Stokes radius of 45 A. The subunit molecular weight of the monomeric valyl-tRNA synthetase is 140,000, as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. In the presence of 400 mM KCl, the purified monomeric valyl-tRNA synthetase associates to a high molecular weight form. The high molecular weight valyl-tRNA synthetase in the homogenate can be readily converted to the monomeric form by controlled trypsinization. The kinetic parameters of the two forms are nearly identical. The results suggest that the high molecular weight valyl-tRNA synthetase is a homotypic tetramer and converts to the monomeric valyl-tRNA synthetase after the cleavage of a small peptide.

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Comparison of the enzymatic behavior of high molecular weight and free lysyl-tRNA synthetase from rat liver: kinetic analysis of lysylation of tRNA

Cited by 6 publications

References 30 publications

Purification of mammalian histidyl-tRNA synthetase and its interaction with myositis-specific anti-Jo-1 antibodies

Purification of mammalian histidyl-tRNA synthetase and its interaction with myositis-specific anti-Jo-1 antibodies

Structural organization of the multienzyme complex of mammalian aminoacyl-tRNA synthetases

Mammalian high-molecular-weight and monomeric forms of valyl-tRNA synthetase

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