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Titolo:
Amino acid sequences and hapten binding of catalytic and noncatalytic antibodies against N-alpha-(5 '-phosphopyridoxyl)-L-lysine
Autore:
Mouratou, B; Gramatikova, S; Kunz, B; Christen, P;
Indirizzi:
Univ Zurich, Inst Biochem, CH-8057 Zurich, Switzerland Univ Zurich Zurich Switzerland CH-8057 chem, CH-8057 Zurich, Switzerland
Titolo Testata:
MOLECULAR IMMUNOLOGY
fascicolo: 11, volume: 37, anno: 2000,
pagine: 633 - 640
SICI:
0161-5890(200008)37:11<633:AASAHB>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSITION-STATE ANALOG; CHEMICAL MODIFICATION; SITES; IMMUNIZATION; DIVERSITY; TYROSINE;
Keywords:
catalytic antibodies; variable domains sequence determination; pyridoxal-5 '-phosphate; chemical modification of antibodies;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Christen, P Univ Zurich, Inst Biochem, Winterthurerstr 190, CH-8057 Zurich, Switzerland Univ Zurich Winterthurerstr 190 Zurich Switzerland CH-8057 nd
Citazione:
B. Mouratou et al., "Amino acid sequences and hapten binding of catalytic and noncatalytic antibodies against N-alpha-(5 '-phosphopyridoxyl)-L-lysine", MOL IMMUNOL, 37(11), 2000, pp. 633-640

Abstract

Upon immunization with a transition-state analog, only a minority of the hapten-binding antibodies will possess catalytic activity, which will vary in efficacy and substrate specificity. Here, the amino acid sequences of thevariable domains of two pyridoxal-5'-phosphate-dependent catalytic and five noncatalytic hapten-binding antibodies raised by immunization with protein-conjugated N-alpha-(5'-phosphopyridoxyl)-L-lysine (Gramatikova, S., Christen, P., 1997. J. Biol. Chem. 272, 9779-9784) were determined by sequencingtheir cDNAs. The analysis revealed that the light chains of this set of antibodies were closely related (pairwise identity 65-80%), whereas the heavychains could be traced back to two different but related groups (intergroup identity 50-54%). The majority of the antibodies proved not to be clonally related, a finding which correlates with their differences in enantiomeric selectivity in ligand binding and reaction specificity. Only one noncatalytic antibody was found to be clonally related with a catalytic antibody, the sequence identity being > 95% in both the V-H and V-L domains. The complementarity-determining regions were invariably abundant in tyrosine residues. Nitration of three to four tyrosine residues with tetranitromethane abolished hapten binding and catalytic activity. Partial protection by pyridoxal-5'-phosphate against inactivation suggested the presence of functionally important tyrosine residues in the binding sites of the antibodies. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 00:25:05