On the Mechanism of Glucose‐6‐Phosphate Dehydrogenase Regulation in Mouse Liver: 2. Purification and Properties of the Mouse‐Liver Enzyme

Amnon Hizi; Gad Yagil

doi:10.1111/j.1432-1033.1974.tb03544.x

On the Mechanism of Glucose‐6‐Phosphate Dehydrogenase Regulation in Mouse Liver: 2. Purification and Properties of the Mouse‐Liver Enzyme

Amnon Hizi^*, Gad Yagil

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

Glucose‐6‐phosphate dehydrogenase is purified from C57BL mouse liver to a specific activity of 116 units/mg protein. The molecular weight of the main active unit is 121000 and it is composed of three interconvertible subforms, as revealed by acrylamide electrophoresis. The main active unit is composed of two subunits of molecular weight 62000, and may aggregate to form higher oligomers. Amino acid composition and dependence of rate on pH and substrate concentration are reported. The kinetic data suggest the existence of two types of active sites with separate sets of K_m and V values. The electrophoretic and kinetic properties of the enzyme from induced and non‐induced liver homogenates are compared.

Original language	English
Pages (from-to)	201-209
Number of pages	9
Journal	European Journal of Biochemistry
Volume	45
Issue number	1
DOIs	https://doi.org/10.1111/j.1432-1033.1974.tb03544.x
State	Published - Jun 1974
Externally published	Yes

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10.1111/j.1432-1033.1974.tb03544.x

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On the Mechanism of Glucose‐6‐Phosphate Dehydrogenase Regulation in Mouse Liver: 2. Purification and Properties of the Mouse‐Liver Enzyme

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