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Titolo:
C-terminal region of VP1 of selected foot-and-mouth disease virus serotypes: Expression in E-coli and affinity purification
Autore:
Ratish, G; Viswanathan, S; Suryanarayana, VVS;
Indirizzi:
Indian Vet Res Inst, Bangalore 560024, Karnataka, India Indian Vet Res Inst Bangalore Karnataka India 560024 24, Karnataka, India
Titolo Testata:
ACTA VIROLOGICA
fascicolo: 4, volume: 43, anno: 1999,
pagine: 205 - 211
SICI:
0001-723X(199908)43:4<205:CROVOS>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYMERASE; PROTEINS; ENZYME;
Keywords:
PCR; diagnostics; FMDV; expressed protein; affinity purification;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Suryanarayana, VVS Indian Vet Res Inst, Bangalore 560024, Karnataka, IndiaIndian Vet Res Inst Bangalore Karnataka India 560024 a
Citazione:
G. Ratish et al., "C-terminal region of VP1 of selected foot-and-mouth disease virus serotypes: Expression in E-coli and affinity purification", ACT VIROLOG, 43(4), 1999, pp. 205-211

Abstract

sFoot-and-mouth disease (FMD), one of the most contagious and economicallyimportant diseases of farm animals, is caused by a FMD virus (FMDV) which belongs to the family of Picornaviridae. The virus occurs as seven serotypes of which four (A, O, C and Asia 1) are prevalent in India. Immunoprophylaxis supported by precise diagnosis is the prime requirement for achieving the success in controlling the disease. Recently, recombinant DNA technologyis gaining importance for the production of cost-effective and safer diagnostics and immunogens. Based on this approach, cDNA of a part of gene for major variable immunogenic region, VPI, of FMBV of four serotypes (A22, O, Cand Asia 1) was amplified by PCR and cloned into expression vector. The expression of the 16 K protein gene from the clones was induced with IPTG andanalyzed by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE) and [S-35]-methionine labeling. The immunoreactivity of the labeled proteins was assayed by immunoprecipitation with anti-FMDV type-specific sera. Since the proteins contain 6 His residues at the N-terminal end their affinity purification was carried out using nickel nitrilo-tri-acetic acid (Ni-NTA) agarose matrix. The proteins were found to be immunoreactive and the useful in the FMD diagnosis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 05:33:20