We produced monoclonal antibodies against the coenzyme pyrrolequinoline quinone (PQQ). These antibodies were obtained by immunizing mice with PQQ conjugated to a chemically modified polypeptide in order to induce a strong immune response. Among the various antibodies obtained, one was found to bind (besides PQQ and 6-hydroxydopamine conjugated to carrier proteins) several different quinoenzymes, namely lentil seedling and bovine serum diamine oxidases and methylamine dehydrogenase. This antibody was able to inhibit the catalytic activity of these enzymes. Moreover, the monoclonal antibody recognized different proteins of lentil seeds on Western blots. Even the variable fragment of immunoglobulin heavy chains of this monoclonal antibody expressed in Escherichia coli is able to recognize the active site of different quinoenzymes.
Marini, S., Giardina, B., Fasciglione, G., FINAZZI AGRO', A. (1993). MONOCLONAL-ANTIBODY RECOGNIZES DIFFERENT QUINONE MOIETIES IN ENZYMES. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 268(18), 13352-13355.
MONOCLONAL-ANTIBODY RECOGNIZES DIFFERENT QUINONE MOIETIES IN ENZYMES
MARINI, STEFANO;FASCIGLIONE, GIOVANNI;FINAZZI AGRO', ALESSANDRO
1993-01-01
Abstract
We produced monoclonal antibodies against the coenzyme pyrrolequinoline quinone (PQQ). These antibodies were obtained by immunizing mice with PQQ conjugated to a chemically modified polypeptide in order to induce a strong immune response. Among the various antibodies obtained, one was found to bind (besides PQQ and 6-hydroxydopamine conjugated to carrier proteins) several different quinoenzymes, namely lentil seedling and bovine serum diamine oxidases and methylamine dehydrogenase. This antibody was able to inhibit the catalytic activity of these enzymes. Moreover, the monoclonal antibody recognized different proteins of lentil seeds on Western blots. Even the variable fragment of immunoglobulin heavy chains of this monoclonal antibody expressed in Escherichia coli is able to recognize the active site of different quinoenzymes.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
