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Archives of biochemistry and biophysics1975; 168(1); 145-162; doi: 10.1016/0003-9861(75)90237-4

Carboxymethyl horse-liver alcohol dehydrogenase. Ligand-binding and kinetic properties of the cysteine-46-modified enzyme.

Abstract: No abstract available
Publication Date: 1975-05-01 PubMed ID: 237472DOI: 10.1016/0003-9861(75)90237-4Google Scholar: Lookup
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APA
Reynolds CH, McKinley-McKee JS. (1975). Carboxymethyl horse-liver alcohol dehydrogenase. Ligand-binding and kinetic properties of the cysteine-46-modified enzyme. Arch Biochem Biophys, 168(1), 145-162. https://doi.org/10.1016/0003-9861(75)90237-4

Publication

ISSN: 0003-9861
NlmUniqueID: 0372430
Country: United States
Language: English
Volume: 168
Issue: 1
Pages: 145-162

Researcher Affiliations

Reynolds, C H
    McKinley-McKee, J S

      MeSH Terms

      • Alcohol Oxidoreductases / metabolism
      • Animals
      • Binding Sites
      • Electrophoresis, Polyacrylamide Gel
      • Electrophoresis, Starch Gel
      • Horses
      • Hydrogen-Ion Concentration
      • Iodoacetates
      • Kinetics
      • Liver / enzymology
      • NAD
      • Oxidation-Reduction
      • Protein Binding
      • Protein Conformation
      • Spectrometry, Fluorescence

      Citations

      This article has been cited 1 times.
      1. Parker DM, Hardman MJ, Plapp BV, Holbrook JJ, Shore JD. pH-dependent changes of intrinsic fluorescence of chemically modified liver alcohol dehydrogenases.. Biochem J 1978 Jul 1;173(1):269-75.
        doi: 10.1042/bj1730269pubmed: 28733google scholar: lookup