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Fructose bisphosphatase from Escherichia coli. Purification and characterization

Archives of Biochemistry and Biophysics

Sep 1, 1983

Jorge Babul, Victoria Guixé

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Abstract

Escherichia coli fructose-1,6-bisphosphatase has been purified for the first time, using a clone containing an approximately 50-fold increased amount of the enzyme. The procedure includes chromatography in phosphocellulose followed by substrate elution and gel filtration. The enzyme has...read more

Mentioned in this Paper

Fructose-1,6-Bisphosphatase
Substrate Specificity
5'-Adenylic Acid
Hydrogen-Ion Concentration
Alkalescens-Dispar Group
Paper Details
References
  • References13
  • Citations24
  • References13
  • Citations24
123

Fructose bisphosphatase from Escherichia coli. Purification and characterization

Archives of Biochemistry and Biophysics

Sep 1, 1983

Jorge Babul, Victoria Guixé

PMID: 6312898

DOI: 10.1016/0003-9861(83)90109-1

Abstract

Escherichia coli fructose-1,6-bisphosphatase has been purified for the first time, using a clone containing an approximately 50-fold increased amount of the enzyme. The procedure includes chromatography in phosphocellulose followed by substrate elution and gel filtration. The enzyme has...read more

Mentioned in this Paper

Fructose-1,6-Bisphosphatase
Substrate Specificity
5'-Adenylic Acid
Hydrogen-Ion Concentration
Alkalescens-Dispar Group

Related Papers

Paper Details
References
  • References13
  • Citations24
  • References13
  • Citations24
123

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