Equine Alcohol Dehydrogenase
| Catalog number: | B2013338 |
| Lot number: | Batch Dependent |
| Expiration Date: | Batch dependent |
| Amount: | 25 mg |
| Molecular Weight or Concentration: | 0.5 U/mg |
| Supplied as: | Powder |
| Applications: | molecular tool for various biochemical applications |
| Storage: | -20C |
| Keywords: | ADH horse |
| Grade: | Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity>18 M-cm) and are filtered through 0.22 um. |
References
- Jrnvall H, von Bahr-Lindstrm H, Jeffery J. Extensive variations and basic features in the alcohol dehydrogenase-sorbitol dehydrogenase family Eur J Biochem. 1984 Apr 2;140(1):17-23.
- Tvrd V, Hruba M, Jirkovsk E, Biedermann D, Kut M, Valentov K, Ken V, Mladnka P. Silymarin Dehydroflavonolignans Chelate Zinc and Partially Inhibit Alcohol Dehydrogenase Nutrients. 2021 Nov 25;13(12):4238.
- Langeland BT, McKinley-McKee JS. The effects of disulfiram on equine hepatic alcohol dehydrogenase and its efficiency against alcoholism: vinegar effect Alcohol Alcohol. 1996 Jan;31(1):75-80.
- Plapp BV, Subramanian R. Alternative binding modes in abortive NADH-alcohol complexes of horse liver alcohol dehydrogenase Arch Biochem Biophys. 2021 Apr 15;701:108825.
- Plapp BV, Savarimuthu BR, Ferraro DJ, Rubach JK, Brown EN, Ramaswamy S. Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis Biochemistry. 2017 Jul 18;56(28):3632-3646.
- Gonnelli M, Strambini GB. The rate of equine liver alcohol dehydrogenase denaturation by urea. Dependence on temperature and denaturant concentration Biophys Chem. 1986 Jul;24(2):161-7.
- Ma Y, Meregalli M, Hodges S, Davies N, Bogdanos DP, Fargion S, Fiorelli G, Vergani D. Alcohol dehydrogenase: an autoantibody target in patients with alcoholic liver disease Int J Immunopathol Pharmacol. 2005 Jan-Mar;18(1):173-82.
- McKie JH, Jaouhari R, Douglas KT, Goffner D, Feuillet C, Grima-Pettenati J, Boudet AM, Baltas M, Gorrichon L. A molecular model for cinnamyl alcohol dehydrogenase, a plant aromatic alcohol dehydrogenase involved in lignification Biochim Biophys Acta. 1993 Sep 3;1202(1):61-9.
- Piersma SR, Visser AJ, de Vries S, Duine JA. Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase Biochemistry. 1998 Mar 3;37(9):3068-77.








