par Giroix, Marie-Hélène;Dufrane, Simon;Sener, Abdullah 
;Malaisse, Willy
Référence Archives internationales de physiologie et de biochimie, 94, page (161-172)
Publication Publié, 1986
;Malaisse, Willy Référence Archives internationales de physiologie et de biochimie, 94, page (161-172)
Publication Publié, 1986
Article révisé par les pairs
| Résumé : | The anomeric specificity of hexokinase was examined in crude homogenates of rat parotid gland, erythrocytes and pancreatic islets. At 8C, the aL/β ratio in maximal velocity averaged 0.73, 0.66 and 0.75 in the parotid, erythrocytes and pancreatic islets, respectively. Hexokinase displayed a greater affinity for aL-than βD-glucose as judged from three criteria: the Km value, the reaction velocity measured with mixtures of the two anomers and their effect upon the phosphorylation of D-[U-14C] glucose in anomeric equilibrium. The latter procedure yielded an aL/β ratio in Km close to 0.51, 0.49 and 0.39 in parotid, erythrocytes and pancreatic islets, respectively. Within the limits of this study, the anomeric specificity of mammalian hexokinase would appear to be a mirror image of that of yeast hexokinase. © 1986 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted. |
