Glucokinase and Hexokinase in Pig Erythrocytes

Fornaini, G; Dachà, Marina; Magnani, Mauro; Fazi, Antonio; Cuppini, C; Bossù, M

doi:10.1159/000458548

Enzyme

1978

DOI: 10.1159/000458548

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Glucokinase and Hexokinase in Pig Erythrocytes

G Fornaini¹,

Marina Dachà²,

Mauro Magnani³

et al.

Abstract: We have shown different enzymatic activities responsible for the phosphorylation of glucose in pig erythrocytes. These activities were observed after partial purification from hemolyzed red cells. One of the enzymes involved is the hexokinase which is present in all tissues; the other is similar to hepatic glucokinase. We have determined the kinetic properties of these activities in hemolysates and in partially purified preparations. Their electrophoretic-migration characteristics were studied too.

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1983

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Cited by 12 publications

References 10 publications

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Molecular forms of red blood cell hexokinase

et al. 1982

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Mammalian red blood cell hexokinase has been shown to exist in two or more distinct molecular forms, which are separable by ion-exchange chromatography. Of these forms just one corresponds to hexokinase type I from other tissues, while the others differ from any previously reported hexokinase isozyme. Analysis of several molecular properties of the three major forms (Ia, Ib and Ic in the order of their elution from DE-52 columns) of hexokinase prepared from human red cells and of the two forms purified from rabbit reticulocytes, shows significant differences in the isoelectric point. The kinetic and regulatory characteristics, the molecular weight, the temperature and pH-dependence of the various isozymes were similar. The hexokinase isozymic pattern is largely dependent upon red blood cell age. Among all, hexokinase Ib is the predominant form in rabbit reticulocytes and becomes the minor component in the older cells; a similar situation has also been found in the human erythrocyte. At present the molecular basis of hexokinase heterogeneity remains unknown, however preliminary experimental findings indicate a post-translational modification as a possible mechanism.

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Molecular forms of red blood cell hexokinase

et al. 1982

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Galactokinase activity and red blood cell age

Magnani

Cucchiarini

Dachà

et al. 1980

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Pig red blood cell hexokinase: Evidence for the presence of hexokinase types II and III, and their purification and characterization

Stocchi

Magnani

Novelli

et al. 1983

Archives of Biochemistry and Biophysics

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Glucokinase and Hexokinase in Pig Erythrocytes

Cited by 12 publications

References 10 publications

Molecular forms of red blood cell hexokinase

Molecular forms of red blood cell hexokinase

Galactokinase activity and red blood cell age

Pig red blood cell hexokinase: Evidence for the presence of hexokinase types II and III, and their purification and characterization

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