Abstract
Heparan sulfate was purified from rat kidney cortex by a combination of affinity chromatography and ion exchange chromatography, and identified by cellulose acetate electrophoresis. As determined by the equilibrium dialysis method, heparan sulfate has two classes of binding sites for dibekacin and gentamicin, and has one class of binding site for amikacin. From the results of equilibrium dialysis using dextran sulfate and hyaluronic acid, the high affinity sites of heparan sulfate for gentamicin and dibekacin were considered to be the sulfate groups, and the low affinity sites to be the carboxyl groups.
