Removal of sialic acids from the purified insulin receptor results in enhanced insulin-binding and kinase activities.

Neuraminidase treatment of the purified insulin receptor resulted in an increase in both insulin-binding and kinase activities. Neuraminidase-treated alpha and beta subunits moved further than native subunits on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions. The enhancement of insulin-binding and kinase activities and increased mobility of the subunits on SDS-PAGE were not observed when the receptor was treated with neuraminidase in the presence of neuraminidase inhibitor. These results suggest that terminal sialic acid residues have a significant role in insulin-binding and kinase activities. The involvement of sialic acid residues in the activities of the receptor has not been detected by previous studies.