Analyze Diet
Archives of biochemistry and biophysics1971; 143(2); 354-358; doi: 10.1016/0003-9861(71)90221-9

Thermal stability of horse liver alcohol dehydrogenase and its complexes.

Abstract: No abstract available
Publication Date: 1971-04-01 PubMed ID: 4326827DOI: 10.1016/0003-9861(71)90221-9Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
  • Journal Article

Cite This Article

APA
Theorell H, Tatemoto K. (1971). Thermal stability of horse liver alcohol dehydrogenase and its complexes. Arch Biochem Biophys, 143(2), 354-358. https://doi.org/10.1016/0003-9861(71)90221-9

Publication

ISSN: 0003-9861
NlmUniqueID: 0372430
Country: United States
Language: English
Volume: 143
Issue: 2
Pages: 354-358

Researcher Affiliations

Theorell, H
    Tatemoto, K

      MeSH Terms

      • Alcohol Oxidoreductases
      • Amides
      • Animals
      • Binding Sites
      • Butyrates
      • Drug Stability
      • Horses
      • Hot Temperature
      • Kinetics
      • Liver / enzymology
      • Mathematics
      • NAD
      • Protein Binding
      • Protein Denaturation
      • Pyrazoles
      • Time Factors

      Citations

      This article has been cited 2 times.
      1. Strambini GB, Gonnelli M. Acrylonitrile quenching of trp phosphorescence in proteins: a probe of the internal flexibility of the globular fold.. Biophys J 2010 Aug 4;99(3):944-52.
        doi: 10.1016/j.bpj.2010.05.022pubmed: 20682273google scholar: lookup
      2. Gonnelli M, Strambini GB. Glycerol effects on protein flexibility: a tryptophan phosphorescence study.. Biophys J 1993 Jul;65(1):131-7.
        doi: 10.1016/S0006-3495(93)81069-5pubmed: 8369422google scholar: lookup