EurekaMag.com logo
+ Translate

Spectral characteristics of asparaginyl and valyl transfer rna synthetases from normal and long fasting rabbit muscles


, : Spectral characteristics of asparaginyl and valyl transfer rna synthetases from normal and long fasting rabbit muscles. Molekulyarnaya Biologiya (Moscow) 18(5): 1330-1335

Conformational differences between asparagyl- and valyl-tRNA synthetases from normal (ARS.eta.) and long-fasting (ARS.intg.) rabbit's muscle were revealed by means of UV fluorescence and differential spectroscopy. The fluorescence spectra indicate more hydrophobic environment of tryptophan residues in the ARS.intg. at similar quantum yields. The differential absorption spectra reveal the distinctions between tryptophanyl microenvironments for ARS's of different amino acid specificity and for ARS.eta. and ARS.intg. of the same specificity. Lower accessibility of tryptophan residues in ARS.eta. in comparison with ARS.intg. was shown by selective fluorescence quenching with Cs+ and I- ions. The effect of longwave shift of fluorescence spectra at the edge excitation was used for studies on microenvironment of chromophors and the rate of the dipole-orientational relaxation of this microenvironment.

(PDF 0-2 workdays service)

Accession: 006459561

Submit PDF Full Text: Here


Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:
Close
Close

Related references

Veselovskaya L.D.; Orlovskaya N.N.; Mnishenko T.I.; Gulyi M.F., 1984: Isolation and purification of aspartyl and valyl transfer rna synthetases from normal and long fasting rabbit muscles their structural peculiarities and some kinetic parameters. Highly purified aspartyl- and valyl-tRNA synthetase were obtained by 6-stage purification from normal and long-fasting rabbit's muscles. The molecular masses of the enzymes are (120 .+-. 10) .cntdot. 103. These proteins consist of 2 subunits...

Veselovskaia, L.D.; Orlovskaia, N.N.; Mnishenko, T.I.; Gulyĭ, M.F., 1984: Isolation and purification of aspartyl- and valyl-tRNA-synthetases from muscles of normal and long-fasting rabbits. Structural characteristics and various kinetic parameters. Highly purified aspartyl- and valyl-tRNA synthetases were obtained by 6-stage purification from normal and long-fasting rabbit's muscles. The molecular masses of the enzymes are (120 +/- 10) X 10(3). These proteins consist of two subunits (al...

Glushak V.N.; Demchenko A.P.; Orlovskaya N.N.; Gulyi M.F., 1984: Spectral characteristics of muscular aspartyl transfer rna synthetases and valyl transfer rna synthetases and their complexes with substrates in norm and after long term starvation. Spectral characteristics of aminoacyl-tRNA-synthetases (ARSase) isolated from muscles of normal rabbits and of those fasted for a long time were studied by fluorescence and differential spectroscopy. Fluorescence spectra and differential absorptio...

Gulyi M.F.; Orlovskaya N.N.; Veselovskaya L.D., 1983: Purification and properties of aspartyl transfer rna synthetase and valyl transfer rna synthetase from muscles of normal and long fasting rabbits. Aspartyl- and valyl-tRNA synthetases were obtained by 7-stage purification from muscle homogenates of normal and long-fasting rabbits. Their molecular mass (110-130 .+-. kilodalton) and subunit structure (.alpha.2-type) were determined by gel-filt...

Gulyi M.F.; Glushak V.N.; Nurbekov N.K., 1984: Limited proteolysis of aspartyl transfer rna synthetase and valyl transfer rna synthetase from muscles of normal and long fasting rabbits. Doklady Akademii Nauk Ukrainskoi SSR Seriya B Geologicheskie Khimicheskie i Biologicheskie Nauki (12): 55-58

Gulyĭ, M.F.; Orlovskaia, N.N.; Veselovskaia, L.D., 1987: Characteristics of the structure and specificity of aspartyl- and valyl-tRNA-synthetases from muscle tissue of long-fasting rabbits. Amino acid compositions of aspartyl- and valyl-tRNA synthetases from the muscles of long-fasting and normal rabbits were studied. Certain differences in amino acid content of fasted and normal rabbits were found. The possibility of incorrect amino...

Glushak, V.N.; Demchenko, A.P.; Orlovskaia, N.N.; Gulyĭ, M.F., 1984: Spectral characteristics of muscle aspartyl- and valyl-tRNA- synthetases and their complexes with substrates in normal conditions and after prolonged starvation. Spectral characteristics of aminoacyl-tRNA-synthetases (ARSases) isolated from muscles of normal rabbits and of those fasted for a long time were studied by the methods of fluorescence and differential spectroscopy. Fluorescence spectra and differ...

Glushak, V.N.; Demchenko, A.P.; Orlovskaia, N.N.; Gulyĭ, M.F., 1984: Spectral characteristics of muscle aspartyl- and valyl-tRNA- synthetases in normal animals and in an experimental model of prolonged starvation. Conformational differences between asparagyl- and valyl-tRNA synthetases from normal (ARSn) and long-fasting (ARSf) rabbit's muscle were revealed by means of UV fluorescence and differential spectroscopy. The fluorescence spectra indicate mor...

Englisch Peters S.; Von Der Haar F.; Cramer F., 1990: Fidelity in the aminoacylation of valyl transfer rna with hydroxy analogues of valine leucine and isoleucine by valyl transfer rna synthetases from saccharomyces cerevisiae and escherichia coli. Several analogues of valine, leucine, and isoleucine carrying hydroxyl groups in the .gamma.- or .delta.-position have been tested in the aminoacylation of tRNA by valyl-tRNA synthetases from Saccharamyces cerevisiae and Escherichia coli. Results...

Jakubowski H., 1983: The poly amine specificity of the valyl transfer rna synthesis reaction catalyzed by prokaryotic escherichia coli and eukaryotic plant lupinus luteus valyl transfer rna synthetases. Bachrach, Uaye And R. Chayen (ed.). Advances In Polyamine Research, Vol. 4. 41st Bat-Sheva Seminar On Polyamines In Growth And Differentiation Processes, Kiryat Anavim, Jerusalem, Israel, July 4-9, . Xxiv 808p. Raven Press: New York, N.y., Usa. Illus. P307-320