PMID: 235298Feb 19, 1975

Glutamate dehydrogenase from Escherichia coli: induction, purification and properties of the enzyme

Biochimica Et Biophysica Acta
F M VeroneseL Conventi

Abstract

When Escherichia coli was grown in a minimum medium with glucose as sole carbon source and a proper level of ammonia, NADP+ specific glutamate dehydrogenase (L-glutamate: NADP+ oxidoreductase (deaminating), ED 1.4.1.4) was induced. The enzyme was solubilized by French press treatment and purified to homogeneity by (NH4)2SO4 fractionation, heat treatment followed by DEAE-cellulose, hydroxylapatite and Bio-Gel chromatography with an overall yield of 30%. The enzyme proved to be heat stable and relatively resistant to protein denaturants. The optimum of enzymic activity for the reductive amination is at pH 8 and at pH 9 for the oxidative deamination. The activity is affected by adenine nucleotides. The molecular weight (about 250 000 for the native form and 46 000 for the inactive subunit) and amino acid composition, suggest strict similarities with the NADP+ enzyme from fungal origin.

References

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Related Concepts

Ammonium Sulfate
Chromatography
Molecular Sieve Chromatography
Enzyme Induction
Alkalescens-Dispar Group
Anhydrous Dextrose
Glutamate Dehydrogenase
Glutamic Acids
Glycerin
Hydrogen-Ion Concentration

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