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
Researcher Affiliations
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.- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- Corran PH, Waley SG. The tryptic peptides of rabbit muscle triose phosphate isomerase.. Biochem J 1974 Apr;139(1):1-10.
- Jörnvall H. Partial similarities between yeast and liver alcohol dehydrogenases.. Proc Natl Acad Sci U S A 1973 Aug;70(8):2295-8.
- 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.
- 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.
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