Two high-affinity monoclonal IgG2a antibodies with differing thermodynamic stability demonstrate distinct antigen-induced changes in protein A-binding affinity

Journal of Immunological Methods

Volumn 217, Issue 1-2, 1998, Pages 131-141

  Kravchuk, Zinaida I ^a   Chumanevich, Alexander A ^a   Vlasov, Alexander P ^a   Martsev, Sergey P ^a  

^a INSTITUTE OF BIOORGANIC CHEMISTRY   (Belarus)

Author keywords

Affinity; Differential scanning calorimetry; IgG2a antibodies; Protein A; Stability

Indexed keywords

FERRITIN; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2A; STAPHYLOCOCCUS PROTEIN A;

ANTIBODY AFFINITY; ANTIBODY COMBINING SITE; ANTIBODY STRUCTURE; ANTIGEN BINDING; ARTICLE; BIOENERGY; COMPETITIVE INHIBITION; CONFORMATIONAL TRANSITION; DIFFERENTIAL SCANNING CALORIMETRY; ENTHALPY; HUMAN; MOLECULAR INTERACTION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; THERMOSTABILITY;

ANIMALS; ANTIBODIES, MONOCLONAL; ANTIBODY AFFINITY; ANTIGEN-ANTIBODY REACTIONS; BINDING, COMPETITIVE; CALORIMETRY, DIFFERENTIAL SCANNING; FERRITINS; HUMANS; IMMUNOGLOBULIN G; MICE; PROTEIN CONFORMATION; PROTEIN DENATURATION; SPLEEN; STAPHYLOCOCCAL PROTEIN A; THERMODYNAMICS;

EID: 0032144264     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(98)00110-0     Document Type: Article

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