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European journal of biochemistry1970; 14(3); 521-534; doi: 10.1111/j.1432-1033.1970.tb00319.x

Horse liver alcohol dehydrogenase. The primary structure of an N-terminal part of the protein chain of the ethanol-active isoenzyme.

Abstract: No abstract available
Publication Date: 1970-07-01 PubMed ID: 4920893DOI: 10.1111/j.1432-1033.1970.tb00319.xGoogle Scholar: Lookup
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  • Journal Article

Cite This Article

APA
Jörnvall H. (1970). Horse liver alcohol dehydrogenase. The primary structure of an N-terminal part of the protein chain of the ethanol-active isoenzyme. Eur J Biochem, 14(3), 521-534. https://doi.org/10.1111/j.1432-1033.1970.tb00319.x

Publication

ISSN: 0014-2956
NlmUniqueID: 0107600
Country: England
Language: English
Volume: 14
Issue: 3
Pages: 521-534

Researcher Affiliations

Jörnvall, H

    MeSH Terms

    • Alcohol Oxidoreductases
    • Amino Acid Sequence
    • Animals
    • Binding Sites
    • Carbon Isotopes
    • Chromatography, Gel
    • Chymotrypsin
    • Crustacea
    • Cyanides
    • Cysteine
    • Ethanol
    • Glyceraldehyde-3-Phosphate Dehydrogenases
    • Horses
    • Iodoacetates
    • Isoenzymes
    • Liver / enzymology
    • Maleates
    • Pepsin A
    • Serine
    • Species Specificity
    • Swine
    • Trypsin
    • Tryptophan
    • Tyrosine

    Citations

    This article has been cited 10 times.
    1. Jörnvall H, Persson M, Jeffery J. Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type.. Proc Natl Acad Sci U S A 1981 Jul;78(7):4226-30.
      doi: 10.1073/pnas.78.7.4226pubmed: 7027257google scholar: lookup
    2. Kunz PA, Loth K, Watterson JG, Schaub MC. Nucleotide induced head-head interaction in myosin.. J Muscle Res Cell Motil 1980 Mar;1(1):15-30.
      doi: 10.1007/BF00711923pubmed: 6453130google scholar: lookup
    3. Bühler R, Hempel J, Kaiser R, von Wartburg JP, Vallee BL, Jörnvall H. Human alcohol dehydrogenase: structural differences between the beta and gamma subunits suggest parallel duplications in isoenzyme evolution and predominant expression of separate gene descendants in livers of different mammals.. Proc Natl Acad Sci U S A 1984 Oct;81(20):6320-4.
      doi: 10.1073/pnas.81.20.6320pubmed: 6387702google scholar: lookup
    4. Brändén CI, Eklund H, Cambillau C, Pryor AJ. Correlation of exons with structural domains in alcohol dehydrogenase.. EMBO J 1984 Jun;3(6):1307-10.
    5. Rex DK, Bosron WF, Li TK. Purification and characterization of mouse alcohol dehydrogenase from two inbred strains that differ in total liver enzyme activity.. Biochem Genet 1984 Feb;22(1-2):115-24.
      doi: 10.1007/BF00499291pubmed: 6370228google scholar: lookup
    6. Orning L, Hammarström S, Samuelsson B. Leukotriene D: a slow reacting substance from rat basophilic leukemia cells.. Proc Natl Acad Sci U S A 1980 Apr;77(4):2014-7.
      doi: 10.1073/pnas.77.4.2014pubmed: 6103542google scholar: lookup
    7. Corran PH, Waley SG. The tryptic peptides of rabbit muscle triose phosphate isomerase.. Biochem J 1974 Apr;139(1):1-10.
      doi: 10.1042/bj1390001pubmed: 4618774google scholar: lookup
    8. Jörnvall H. Partial similarities between yeast and liver alcohol dehydrogenases.. Proc Natl Acad Sci U S A 1973 Aug;70(8):2295-8.
      doi: 10.1073/pnas.70.8.2295pubmed: 4599620google scholar: lookup
    9. Brändén CI, Eklund H, Nordström B, Boiwe T, Söderlund G, Zeppezauer E, Ohlsson I, Akeson A. Structure of liver alcohol dehydrogenase at 2.9-angstrom resolution.. Proc Natl Acad Sci U S A 1973 Aug;70(8):2439-42.
      doi: 10.1073/pnas.70.8.2439pubmed: 4365379google scholar: lookup
    10. Rex DK, Bosron WF, Dwulet F, Li TK. Purification and characterization of the Danish (Skive) variant of mouse liver alcohol dehydrogenase.. Biochem Genet 1987 Feb;25(1-2):111-21.
      doi: 10.1007/BF00498955pubmed: 3579863google scholar: lookup