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PMID:16385241

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Citation

Negoro, M and Wakabayashi, I (2005) Interactions of alcohol dehydrogenase to p-hydroxyacetophenone-sepharose and p-acetamidophenol-sepharose. Alcohol. Clin. Exp. Res. 29:304S-8S

Abstract

p-Hydroxyacetophenone (HAP)-sepharose is known to be an effective ligand for isolation of aldehyde dehydrogenase and chloramphenicol acetyltransferase. In this study, we investigated ligand specificities to alcohol dehydrogenase (ADH) using p-HAP-sepharose and p-acetamidophenol (AAP)-sepharose.

Links

PubMed

Keywords

Acetaminophen/chemistry; Acetophenones/chemistry; Alcohol Dehydrogenase/chemistry; Animals; Chromatography, Affinity; Chromatography, High Pressure Liquid; Cytosol/enzymology; Electrophoresis, Polyacrylamide Gel; Horses; Liver/enzymology; Male; Rats; Rats, Wistar; Sepharose/chemistry; Sequence Analysis, Protein

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

RAT:ADH1

located_in

GO:0005829: cytosol

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

RAT:ADH1

enables

GO:0097159: organic cyclic compound binding

ECO:0000353: physical interaction evidence used in manual assertion

CHEBI:28032
CHEBI:46195

F

Seeded From UniProt

complete

RAT:ADH1

part_of

GO:0005829: cytosol

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

RAT:ADH1

enables

GO:0008144: drug binding

ECO:0000353: physical interaction evidence used in manual assertion

PubChem_Compound:7469

F

Seeded From UniProt

complete


See also

References

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