Influence of antibody binding on oxygen binding behavior of Panulirus interruptus hemocyanin

• Published in: FEBS letters Vol. 408; no. 2; pp. 124 - 126
• Main Authors: Perton, Frank G, Beintema, Jaap J, Decker, Heinz
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 19.05.1997
• Subjects: Animals; Antibodies, Monoclonal - immunology; antigen binding fragment obtained by digestion of immunoglobulin with papain; Cooperativity; Epitopes - chemistry; Epitopes - immunology; Fab; Hemocyanin; Hemocyanins - chemistry; Hemocyanins - immunology; Hemocyanins - metabolism; Immunoglobulin Fab Fragments - immunology; Marine; Monoclonal antibodies; Nephropidae; Oxygen - metabolism; Oxygen binding; Panulirus interruptus; Protein Binding; Protein Conformation; Monoclonal antibodies; Cooperativity; F ab; Hemocyanin; Panulirus interruptus; Oxygen binding
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(97)00269-X

Oxygen binding behavior of monomeric subunit a and the hexameric form of this subunit of hemocyanin of Panulirus interruptus is influenced by the binding of various monoclonal antibodies. These antibodies react with other surface parts of the subunit than its second domain in which the oxygen binding site is located. The influence of three monoclonal antibodies and their antigen binding fragments (F ab) has been investigated. Two antibodies increase the oxygen affinity of monomeric hemocyanin from that observed in its low affinity T-state, while the third has little influence on this property. F ab fragments abolish almost completely the cooperativity of oxygen binding by the hexameric hemocyanin molecule. The two antibodies which increase the oxygen affinity of the monomeric molecule stabilize high-affinity states of the hexameric molecule, while the third stabilizes the low-affinity state.