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Thermodynamics of Antigen‐antibody Binding using Specific Anti‐lysozyme Antibodies

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

European journal of biochemistry, 1995-03, Vol.228 (2), p.388-394 [Periódico revisado por pares]

Oxford, UK: Blackwell Science Ltd

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  • Título:
    Thermodynamics of Antigen‐antibody Binding using Specific Anti‐lysozyme Antibodies
  • Autor: Schwarz, Frederick P. ; Tello, Diana ; Goldbaum, Fernando A. ; Mariuzza, Roy A. ; Poljak, Roberto J.
  • Assuntos: Antigen‐antibody binding ; hydrogen bonding ; lysozyme ; thermodynamics ; titration calorimetry
  • É parte de: European journal of biochemistry, 1995-03, Vol.228 (2), p.388-394
  • Descrição: Titration calorimetry measurements on the binding of hen lysozyme to the specific monoclonal IgG antibodies D1.3, D11.15, D44.1, F9.13.7, F10.6.6, their papain‐cleaved antigen binding fragments (Fab) and their protein‐engineered fragments consisting of non‐covalently linked heavy variable chain and light variable chain domains (Fv) were performed between 6–50°C in 0.15 M NaCl, 0.01 M sodium phosphate pH7.1. The binding thermodynamic free energy change (ΔGbo), enthalpy change (ΔHb), and entropy change (ΔSb) were the same for the whole IgG and its Fv and Fab fragments. With the exception of F9.13.7 at 13 °C, all the binding reactions were enthalpically driven with enthalpy changes ranging from −129 ± 7 kJmol−1 (D1.3 at 49.8°C) to −26.2 ± 0.6 kJ mol−1 (D44.1 at 8.0°C). The heat capacity changes for the binding reaction (ΔCp) ranged from −2.72 ± 0.16 kJ mol−1 K−1 (F9.13.7) to −0.95 ± 0.06 kJ mol−1 K−1 (F10.6.6). The apolar surface areas buried at the binding sites estimated from the heat capacity changes indicate that the binding reactions are primarily hydrophobic, contrary to the mainly observed enthalpy‐driven nature of the reactions. Conformational stabilization and the presence of water at the antigen‐antibody interface may account for this discrepancy.
  • Editor: Oxford, UK: Blackwell Science Ltd
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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