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Titolo:
Characterization of monoclonal antibodies against ascorbate peroxidase isoenzymes: purification and epitope-mapping using immunoaffinity column chromatography
Autore:
Yoshimura, K; Ishikawa, T; Wada, K; Takeda, T; Kamata, Y; Tada, T; Nishimura, K; Nakano, Y; Shigeoka, S;
Indirizzi:
Kinki Univ, Fac Agr, Dept Food & Nutr, Nara 6318505, Japan Kinki Univ Nara Japan 6318505 Agr, Dept Food & Nutr, Nara 6318505, Japan Shimane Univ, Fac Life & Environm Sci, Matsue, Shimane 6908504, Japan Shimane Univ Matsue Shimane Japan 6908504 Matsue, Shimane 6908504, Japan Univ Osaka Prefecture, Adv Sci & Technol Res Inst, Osaka 5998570, Japan Univ Osaka Prefecture Osaka Japan 5998570 Res Inst, Osaka 5998570, Japan Univ Osaka Prefecture, Dept Vet Sci, Coll Agr, Osaka 5998570, Japan Univ Osaka Prefecture Osaka Japan 5998570 Coll Agr, Osaka 5998570, Japan Univ Osaka Prefecture, Dept Appl Biochem, Osaka 5998570, Japan Univ Osaka Prefecture Osaka Japan 5998570 Biochem, Osaka 5998570, Japan
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
fascicolo: 2, volume: 1526, anno: 2001,
pagine: 168 - 174
SICI:
0304-4165(20010503)1526:2<168:COMAAA>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR CHARACTERIZATION; SPINACH; CHLOROPLASTS; EXPRESSION; LEAVES; ISOZYMES; PROTEIN; STRESS;
Keywords:
ascorbate peroxidase; isoenzyme; recombinant enzyme; monoclonal antibody; epitope;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Shigeoka, S Kinki Univ, Fac Agr, Dept Food & Nutr, 3327-204 Nakamachi, Nara 6318505, Japan Kinki Univ 3327-204 Nakamachi Nara Japan 6318505 18505, Japan
Citazione:
K. Yoshimura et al., "Characterization of monoclonal antibodies against ascorbate peroxidase isoenzymes: purification and epitope-mapping using immunoaffinity column chromatography", BBA-GEN SUB, 1526(2), 2001, pp. 168-174

Abstract

We have developed three monoclonal antibodies against spinach chloroplastic (chl-mAb3 and chl-mAb6) and cytosolic (cyt-mAb1) ascorbate peroxidase (APX) isoenzymes to analyze the cross-reactivity and the structure of the epitopes for each monoclonal antibody. All three antibodies reacted specifically with their respective isoenzymes, but non cross-reacted with the others. Immunoreactive fragments in proteolytic recombinant APX isoenzymes were detected by means of the absorption on the corresponding immunoaffinity column. The cyt-mAb1 reacted with a peptide fragment containing the distal His region obtained by the lysyl endopeptidase digestion. The chl-mAb6 was capable of binding to the fragment. D-I-K-E-K-R, which is consistent with an inherent region of chloroplastic isoenzymes. No fragments reacting to the chl-mAb3 could be found in this study, suggesting that the chl-mAb3 recognizes aconformationally constituted epitope of the chloroplastic APX molecule, which may be destroyed by the enzymatic cleavage. We concluded that the peptides identified as epitope are characteristic evidence of monoclonal antibodies. (C) 2001 Published by Elsevier Science B.V.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 17:13:25