CONDENSATION OF DEXTRAN-DIALDEHYDE WITH AMINO-ACIDS UNDER NONREDUCTIVE CONDITIONS

The reaction between dextran-dialdehyde, prepared by periodate oxidation, and glycine was examined in detail. In contrast to that of aldose with amino acids, the dialdehyde reaction proceeded very rapidly. Higher temperatures and Ph were favorable for the reaction and the initial velocity was proportional to the reaction time and the concentration of dextran-dialdehyde. Although the dextran-glycine adduct was stable during the gel filtration step to remove excess glycine, the adduct was readily dissociated by 0.3 M HCl. Among the amino acids tested, histidine and glycine gave higher reactivity than lysine and arginine. This basic information is useful for condensation of dextran-dialdehyde with various proteins and enzymes.