Mechanism of coupling periodate-oxidized nucleosides to proteins.
This paper describes a mechanism of coupling periodate-oxidized nucleosides to proteins. Each of the dialdehyde groups of a periodate-oxidized nucleoside is shown to couple to lysine residues on different protein molecules through Schiff bases, thereby cross-linking different protein molecules, forming a polymer. This is in contrast to the previous model in which nucleosides were suggested to couple to proteins through a morpholine structure. The cross-linked structure of the nucleoside-antigen, significantly different when compared to the native protein, may affect the specificity and the efficiency of antibody production.
D000917:Antibody Formation; D001665:Binding Sites; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D009025:Morpholines; D009705:Nucleosides / Q000276:immunology*; D010084:Oxidation-Reduction; D010504:Periodic Acid; D011485:Protein Binding; D011506:Proteins / Q000276:immunology*; D012545:Schiff Bases; D012710:Serum Albumin, Bovine / Q000276:immunology
D009025:Morpholines; D009705:Nucleosides; D011506:Proteins; D012545:Schiff Bases; D010504:Periodic Acid; D012710:Serum Albumin, Bovine