Résumé : In both rat parotid gland and pancreatic islet homogenates, the rate of glucose phosphorylation is higher with β- than α-D-[U-14C]glucose (0.5 mM). Glucose 6-phosphate (25 to 300 μM), in anomeric equilibrium, exerts a more marked inhibitory effect upon α- than β-D-[U-14C]glucose phosphorylation. In the absence and presence of glucose 6-phosphate, hexokinase displays a greater affinity for α- than β-D-glucose. Except for the latter feature, the properties of hexokinase thus favour the phosphorylation of the β-anomer of glucose.