Biopolym. Cell. 1990; 6(5):65-72.
http://dx.doi.org/10.7124/bc.00028F
Structure and Function of Biopolymers
Studies of seryl-tRNA-synthetase from the bovine liver by the immunochemical methods
1Sidorik L. L., 1Gudzera O. I., 2Zolotukhina I. M., 2Dragovoz V. A., 1Tukalo M. A., 2Beresten S. F., 1Matsuka G. Kh.
  1. Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR
    Kiev, USSR
  2. Engelhardt Institute of Molecular Biology, Academy of Sciences of the USSR
    Moscow, USSR

Abstract

Polyclonal affined-purified antibodies against bovine seryl-tRNA-synthetase were prepared. Antibodies inhibit the Ser-tRNA synthetase activity and interact with the seryl-tRNA-synthetases from different organisms. Antibodies cross-react with seryl-tRNA-synthetases of eucaryotic rather than procaryotic species, as revealed by immunoblot analysis.
Full text: (PDF, in Russian)

References

[1] Kiselev LL, Favorova OO, Lavrik OI. Biosynthesis of proteins from amino acid to the aminoacyl-tRNA. Moscow, Nauka, 1984; 408 p.
[2] Beresten SF, Zargarova TA, Favorova OO, Rubikaite BI, Ryazanov AG, Kisselev LL. Molecular and cellular studies of tryptophanyl-tRNA synthetase using monoclonal antibodies. Evaluation of a common antigenic determinant in eukaryotic, prokaryotic and archaebacterial enzymes which maps outside the catalytic domain. Eur J Biochem. 1989;184(3):575-81.
[3] Beresten' SF, Zargarova TA, Kostrov SV, Favorova OO. Monoclonal antibodies against tryptophanyl-tRNA-synthetase. Mol Biol (Mosk). 1984;18(5):1407-11.
[4] Gudzera OI, Sidorik LL, Zolotukhina IV, Tukalo MA, Matsuka GKh. Isolation of seryl-tRNA synthetase from the animal liver by proximate method. Biopolym Cell. 1990; 6(2):105-7.
[5] Beresten' SF, SheÄ­nker VSh, Rokhlin OV. Immunochemical properties of tryptophanyl-tRNA synthetase and its fragments. Mol Biol (Mosk). 1978;12(6):1408-19.
[6] Favorova OO, Zargarova TA, Rukosuev VS, Beresten SF. Species and tissue-specific variations in distribution of mammalian tryptophanyl-tRNA synthetase: an abnormal high content in bovine pancreas. Biopolym Cell. 1988; 4(6):290-7.
[7] Popenko VI, Cherni NE, Beresten' SF, Zargarova TA, Favorova OO. Immune electron microscope determination of the localization of tryptophanyl-tRNA-synthetase in bacteria and higher eukaryotes. Mol Biol (Mosk). 1989;23(6):1669-81.
[8] Zargarova TA, Beresten' SF, Favorova OO, Kiselev LL. Tryptophanyl-tRNA-synthetases of eukaryotes, prokaryotes and archebacteria have a common antigenic determinant. Dokl Akad Nauk SSSR. 1985;285(6):1484-6.
[9] Beresten SF, Rubikaite BI, Kazakov VK. Localization of antigenic determinants of beef tryptophanyl-tRNA synthetase revealed by monoclonal antibodies. Biopolym Cell. 1987; 3(2):59-65.
[10] Scheinker VS, Beresten SF, Mazo AM, Ambartsumyan NS, Rokhlin OV, Favorova OO, Kisselev LL. Immunochemical studies of beef pancreas tryptophanyl-tRNA synthetase and its fragments. Determination of the number of antigenic determinants and a comparison with tryptophanyl- tRNA synthetases from other sources and with reverse transcriptase from avian myeloblastosis virus. Eur J Biochem. 1979;97(2):529-40.
[11] Beresten SF, Rubikaite BI, Kisselev LL. A general approach to the localization of antigenic determinants of a linear type in proteins of unknown primary structure. J Immunol Methods. 1988;113(2):247-54.
[12] Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964;91(2):222-33.
[13] Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.
[14] Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72:248-54.
[15] Baily G. S. The production of Antisera. Meth. Mol. Biol. New York, 1984:295-300.
[16] Methods in immunology. Ed. G Freemel. Moscow, Medicine, 1987; 472 p.
[17] Goosen PC. Isolation of subclasses of human IgG with affinity chromatography. J Immunol Methods. 1980;37(1):89-93.
[18] Engel G, Heider H, Maelicke A, von der Haar F, Cramer F. Fluorescence studies on substrate binding to seryl-tRNA synthetase from yeast. Eur J Biochem. 1972;29(2):257-62.
[19] Heider H, Gottschalk E, Cramer F. Isolation and characterization of seryl-tRNA synthetase from yeast. Eur J Biochem. 1971;20(1):144-52.
[20] Pingoud A, Riesner D, Boehme D, Maass G. Kinetic studies on the interaction of seryl-tRNA synthetase with tRNASer and ser-tRNAser from yeast. FEBS Lett. 1973;30(1):1–5.
[21] Bruton C. J. Probing the sub-structure, evolution and interactions of aminoacyl-tRNA synthetases. Nonsence mutations and tRNA suppressors. Eds J. E. Selis, J. D. Smith -New York: Acad, press, 1979:47-68.
[22] Eigen M. Selforganization of matter and the evolution of biological macromolecules. Naturwissenschaften. 1971;58(10):465-523.