Biopolym. Cell. 1990; 6(4):97-101.
Gene-Engineering Biotechnology
A method for selection of hybridomas, secreting monoclonal antibodies against tyrosyl-tRNA synthetase, based on monitoring of the enzymatic activity
1Ribkinska T. A., 2Vartanyan O. A., 1Filonenko V. V., 1Sidorik L. L., 1Kornelyuk A. I., 2Beresten S. F.
- Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR
Kiev, USSR - Engelhardt Institute of Molecular Biology, Academy of Sciences of the USSR
Moscow, USSR
Abstract
A new method for screening populations of hybrid cells secreting monoclonal antibodies (Mabs) against aminnacyl-tRNA synthetases (ARS) is developed as based on monitoring of the enzymatic activity of ARSes. The main advantage of this procedure stems from the fact that it permits using non-homogeneous ARS preparations both for immunization and for screening. While applying this procedure, hybridoma cell line T3 secreting Mabs against bovine tyrosyl-tRNA synthetase has been produced and characterized.
Full text: (PDF, in Russian)
References
[1]
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.
[2]
Filonenko VV, Beresten SF, Rubikaite BI, Kisselev LL. Bovine tryptophanyl-tRNA synthetase and glyceraldehyde-3-phosphate dehydrogenase form a complex. Biochem Biophys Res Commun. 1989;161(2):481-8.
[3]
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.
[4]
Sallafranque ML, Garret M, Benedetto JP, Fournier M, Labouesse B, Bonnet J. Tryptophanyl-tRNA synthetase is a major soluble protein species in bovine pancreas. Biochim Biophys Acta. 1986;882(2):192-9.
[5]
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.
[6]
Kovaleva GK, Merkulova TI, Nurbekov MK, Kholmuratov EG. Covalent derivatives of aminoacyl-tRNA-synthetases with substrates. Mol Biol (Mosk). 1984;18(5):1412-8.
[7]
Kearney JF, Radbruch A, Liesegang B, Rajewsky K. A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines. J Immunol. 1979;123(4):1548-50.
[8]
Engvall E, Perlmann P. Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin G. Immunochemistry. 1971;8(9):871-4.
[9]
Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.
[10]
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. Russian.
