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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Magnani M, Cucchiarini L, Stocchi V, Bossu M, Dacha M, Fornaini G

Istituto di Chimica Biologica, Università degli Studi di Urbino, Italy.

Comp Biochem Physiol B. 1979;64(3):267-71. doi: 10.1016/0305-0491(79)90141-x.

ATP: D-galactose-1-phosphotransferase activity was measured in human, pig, cow, rabbit, mouse and rat red blood cells. Mean values of galactokinase activity was markedly lower in the human and pig erythrocyte as compared to those of the other species. 2. The permeability to galactose of the red cells studied was always higher than galactose phosphorylation. 3. The affinity constants of galactokinase for galactose ranged from 119 to 291 microM and from 178 to 406 microM for ATPMg2-. 4. The thermostability values of the galactokinase of the species studied were similar. The pH-optimum is pH 7.5 for the human, mouse and rabbit enzyme and pH 8.0 for cow, pig and rat galactokinase.

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Magnani M, Cucchiarini L, Stocchi V, Bossu M, Dacha M, Fornaini G

Istituto di Chimica Biologica, Università degli Studi di Urbino, Italy.

Comp Biochem Physiol B. 1979;64(3):267-71. doi: 10.1016/0305-0491(79)90141-x.

ATP: D-galactose-1-phosphotransferase activity was measured in human, pig, cow, rabbit, mouse and rat red blood cells. Mean values of galactokinase activity was markedly lower in the human and pig erythrocyte as compared to those of the other species. 2. The permeability to galactose of the red cells studied was always higher than galactose phosphorylation. 3. The affinity constants of galactokinase for galactose ranged from 119 to 291 microM and from 178 to 406 microM for ATPMg2-. 4. The thermostability values of the galactokinase of the species studied were similar. The pH-optimum is pH 7.5 for the human, mouse and rabbit enzyme and pH 8.0 for cow, pig and rat galactokinase.