Biopolym. Cell. 1991; 7(5):33-36.
Structure and Function of Biopolymers
The immunochemical approach for studies of structure tyrosyl-tRNA synthetase from bovine liver
1Ribkinska T. A., 1Kornelyuk A. I., 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

The antigenic determinant for mAbs T3 against tyrosyl-tRNA synthetase from bovine liver has been localized outside of the active site of enzyme. This epitope also remains for the active truncated enzyme form (dimer of 39 kDa subunits) product by limited endogenous proteolysis. The tyrosyl-tRNA synthetases of higher eukaryotes (bovine liver, rabbit liver, human placenta) have the common antigenic determinant, which lacks in tyrosyl-tRNA synthetases from prokaryots (E. coli, Th. thermophilus) and from yeast as revealed by immunoblot analysis.

References

[1] 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.
[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] Korneliuk AI, Kurochkin IV, Matsuka GKh. Tyrosyl-tRNA synthetase from the bovine liver. Isolation and physico-chemical properties. Mol Biol (Mosk). 1988;22(1):176-86.
[4] Kurochkin IV, Ribkinska TA, Gnatenko DV et al. Tyrosyl-tRNA synthetases from beef liver: generation of multiple enzyme forms by endogenous proteolysis. Int. seminar on interferon and biotechnol.: Abstr. Havana, 1989:S06-066.
[5] Ribkinska TA, Vartanyan OA, Filonenko VV, Sidorik LL, Kornelyuk AI, Beresten SF. A method for selection of hybridomas, secreting monoclonal antibodies against tyrosyl-tRNA synthetase, based on monitoring of the enzymatic activity. Biopolym Cell. 1990; 6(4):97-101
[6] 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.
[7] Prast system owners manual (Pharmacia). Uppsala, 1987. 10 p.
[8] Beresten' SF, Zargarova TA, Kostrov SV, Favorova OO. Monoclonal antibodies against tryptophanyl-tRNA-synthetase. Mol Biol (Mosk). 1984;18(5):1407-11.
[9] Deák F, Dénes G. Purification and some properties of rat liver tyrosyl-tRNA synthetase. Biochim Biophys Acta. 1978;526(2):626-34.
[10] Prasada Rao YS, Srinivasan PR. Purification and properties of tyrosyl tRNA synthetase of rat liver. Nucleic Acids Res. 1977;4(11):3887-900.
[11] Takahashi R, Goto S. Fidelity of aminoacylation by rat-liver tyrosyl-tRNA synthetase. Effect of age. Eur J Biochem. 1988;178(2):381-6.