Cytochemistry of colloidal iron binding to the surface of Hela cells and human erythrocytes.
It seems from the literature that colloidal iron (C.I.) binding sites on cell surfaces cannot be completely removed by treatment with Vibrio Colerae alpha-neuraminidase. We wondered if C.I. particles bind to negative groups other than the carboxyl groups of sialic acids. Using HeLa cells from suspension cultures and fresh human erythrocytes, we examined, with the transmission electronmicroscope, the influence of the following enzymatic and histochemical treatments on C.I. staining: alpha-neuraminidase; hyaluronidase; ribonuclease; alpha-amylase; mild methylation (MM); MM + saponification (Sap.); MM + Sap +MM; MM + Sap + alpha-neuraminidase; active methylation (AM); AM + Sap; AM + Sap + AM; AM + Sap + alpha-neuraminiadase; CH3OH (80%); Sap. It seemed from these experiments that the carboxyl groups of alpha-neuraminidase sensitive sialic acids constitute the majority of binding sites for C.I. to these particular cells. The most interesting candidates for the residual binding of C.I. are carboxyl groups of alpha-neuraminidase resistant molecules, sulfon, sulfin, and sulfate groups.
D001665:Binding Sites; D002264:Carboxylic Acids / Q000032:analysis; D003102:Colloids; D004910:Erythrocyte Membrane / Q000032:analysis* / Q000648:ultrastructure; D004912:Erythrocytes / Q000032:analysis*; D006367:HeLa Cells / Q000032:analysis; D006801:Humans; D007501:Iron / Q000378:metabolism; D009439:Neuraminidase; D012794:Sialic Acids / Q000032:analysis*; D013194:Staining and Labeling
D002264:Carboxylic Acids; D003102:Colloids; D012794:Sialic Acids; D007501:Iron; D009439:Neuraminidase