Effect of monoclonal antibodies in preventing carboxypeptidase A aggregation.

摘要: With an increase in temperature, carboxypeptidase A shows a decrease solubility that is accompanied by loss of enzymic activity and conformational changes leading to its aggregation. In the present study we investigated suppression enzyme aggregation via interaction with two monoclonal antibodies raised against native protein. The protein process was monitored ELISA measurements determination residual activity. As previously found, selected which do not inhibit biological antigen bind similar affinity constant their epitopes on molecule exhibit chaperone-like refolding antigen. These have inhibitory effect seems be related location antigenic site recognized each antibody. Identifying aggregating epitopes' as sequences are sites where initiated preparing these regions may facilitate understanding prevention protein-aggregation processes.