[Purification and properties of cytoplasmic and mitochondrial hexokinase from the rabbit brain].
The soluble Hexokinase from rabbit brain was purified 4,700-fold to near homogeneity by a combination of ion-exchange chromatography, dye-ligand chromatography and affinity chromatography. The purified enzyme showed a specific activity of 110 units/mg of protein and was obtained in 70% yield. The properties of the purified cytoplasmic hexokinase were compared with those of the solubilized mitochondrial enzyme. No significant differences were found in M.W., pI and electrophoretic mobility. However, the temperature dependence of activity and specificity for several hexose substrates were markedly different.
D000818:Animals; D001921:Brain / Q000201:enzymology* / Q000648:ultrastructure; D003593:Cytoplasm / Q000201:enzymology; D006593:Hexokinase / Q000302:isolation & purification*; D007526:Isoelectric Point; D008928:Mitochondria / Q000201:enzymology; D008970:Molecular Weight; D011817:Rabbits; D013696:Temperature
D006593:Hexokinase
Purificazione e proprieta' dell'esocinasi citoplasmatica e di quella mitocondriale da cervello di coniglio.