Idioma:

Structural and physicochemical analysis of the reaction between the anti-lysozyme antibody D1.3 and the anti-idiotopic antibodies E225 and E5.2

Tello, Diana ; Eisenstein, Edward ; Schwarz, Frederick P. ; Goldbaum, Fernando A. ; Fields, Barry A. ; Mariuzza, Roy A. ; Poljak, Roberto J.

Journal of molecular recognition, 1994-03, Vol.7 (1), p.57-62 [Periódico revisado por pares]

Chichester, UK: John Wiley & Sons, Ltd

Sem texto completo

Citações Citado por

Enviar para

Título:
Structural and physicochemical analysis of the reaction between the anti-lysozyme antibody D1.3 and the anti-idiotopic antibodies E225 and E5.2
Autor: Tello, Diana ; Eisenstein, Edward ; Schwarz, Frederick P. ; Goldbaum, Fernando A. ; Fields, Barry A. ; Mariuzza, Roy A. ; Poljak, Roberto J.
Assuntos: Animals ; Antibodies, Anti-Idiotypic - immunology ; Antibodies, Monoclonal - immunology ; Antibody Affinity ; Antigen-Antibody Reactions ; Binding Sites, Antibody ; Calorimetry ; Chemical Phenomena ; Chemistry, Physical ; Conformational change ; Enthalpy and entropy ; Idiotypes ; Mice ; Mice, Inbred BALB C ; Models, Molecular ; Monoclonal antibodies ; Muramidase - immunology ; Protein Binding ; Protein Conformation ; Thermodynamics ; Ultracentrifugation
É parte de: Journal of molecular recognition, 1994-03, Vol.7 (1), p.57-62
Notas: ArticleID:JMR300070108
ark:/67375/WNG-L0X8PD98-V
istex:D59A931558EA1038AB8EDC33F79FAE9551CD6211
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: The reaction between the mouse (BALB/c) anti‐idiotiopic monoclonal antibodies E225 and E5.2 and idiotopes on the (BALB/c) anti‐lysozyme monoclonal antibody D1.3 has been characterized by titration calorimetry, by equilibrium sedimentation and by the determination of binding association and dissociation rates. The reaction between E5.2 and D1.3 is driven by a large negative enthalpy and its rate and equilibrium association constants are comparable to those observed in other antigen–antibody reactions. In contrast, the reaction between E225 and D1.3 is entropically driven and characterized by slow association kinetic (1 × 103 M−1 sec−1) and a resulting low equilibrium constant (Ka = 2 × 105M−1). A correlation of these properties with the three‐dimensional structure of the Fab225‐FabD1.3 complex, previously determined by X‐ray diffraction methods to 2.5 Å resolution, indicates that conformational changes of several D1.3 contacting residues, located in its complementarity determining regions, may explain these features of the reaction.
Editor: Chichester, UK: John Wiley & Sons, Ltd
Idioma: Inglês

Links

View this record in MEDLINE/PubMed

Voltar para lista de resultados

Realização: Logos de Redes Sociais:

Structural and physicochemical analysis of the reaction between the anti-lysozyme antibody D1.3 and the anti-idiotopic antibodies E225 and E5.2

Tello, Diana ; Eisenstein, Edward ; Schwarz, Frederick P. ; Goldbaum, Fernando A. ; Fields, Barry A. ; Mariuzza, Roy A. ; Poljak, Roberto J.

Chichester, UK: John Wiley & Sons, Ltd

Buscando em bases de dados remotas. Favor aguardar.