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PMID: 4401601 Published · ppublish English Journal Article

Glucose-6-phosphate dehydrogenase from Escherichia coli and from a "high-level" mutant.

Journal of bacteriology ·Vol. 110 ·No. 1 ·1972-04-00 ·Pages 155-60

Banerjee S, Fraenkel DG

Abstract

Glucose-6-phosphate dehydrogenase has been purified to near homogeneity from wild-type Escherichia coli K-12 and from a mutant previously found to contain substantially more of the enzyme. The two enzymes are the same in all characteristics studied thus far: specific activity, kinetics, specificity, and subunit size.

MeSH Terms
Adenosine Triphosphate Aluminum Silicates Chromatography Chromatography, DEAE-Cellulose Electrophoresis, Disc Enzyme Activation Escherichia coli/enzymology Genetics, Microbial Glucosephosphate Dehydrogenase/antagonists & inhibitors,isolation & purification Hydrogen-Ion Concentration Hydroxyapatites Kinetics Macromolecular Substances Magnesium Mutation NAD NADP Sodium Dodecyl Sulfate
Chemicals
Aluminum Silicates Hydroxyapatites Macromolecular Substances NAD Sodium Dodecyl Sulfate NADP Adenosine Triphosphate Glucosephosphate Dehydrogenase Magnesium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Banerjee S
Fraenkel D G
References (21)
21 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.110.1.155-160.1972
Published
1972-04-00
Pages
155-60
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC247392
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.110.1.155-160.1972 PMC Full Text View journal details
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