The half-of-the-sites reactivity of horse liver alcohol dehydrogenase in the presence of alcohol substrates
- PMID: 4375199
- DOI: 10.1016/0022-2836(74)90415-x
The half-of-the-sites reactivity of horse liver alcohol dehydrogenase in the presence of alcohol substrates
Similar articles
-
Evidence for site equivalence in the reaction mechanism of horse liver alcohol dehydrogenase with aromatic substrates at alkaline pH.Biochemistry. 1977 Jun 28;16(13):2961-22. doi: 10.1021/bi00632a018. Biochemistry. 1977. PMID: 18165 No abstract available.
-
Binding of NADH to horse liver alcohol dehydrogenase: dependence on concentration of benzaldehyde and benzyl alcohol.Physiol Chem Phys Med NMR. 1984;16(1):21-7. Physiol Chem Phys Med NMR. 1984. PMID: 6385034
-
The use of steady-state treatment in the rapid kinetics of horse liver alcohol dehydrogenase. The evaluation of data on the amplitude of the "burst" reaction.Arch Biochem Biophys. 1975 Jan;166(1):16-24. doi: 10.1016/0003-9861(75)90359-8. Arch Biochem Biophys. 1975. PMID: 235887 No abstract available.
-
Mammalian liver alcohol dehydrogenases.Adv Exp Med Biol. 1975;56:1-31. doi: 10.1007/978-1-4684-7529-6_1. Adv Exp Med Biol. 1975. PMID: 167554 Review.
-
Synthesis and properties of some new NAD analogues.Top Curr Chem. 1974;52:209-33. doi: 10.1007/3-540-06873-2_18. Top Curr Chem. 1974. PMID: 4376282 Review. No abstract available.
Cited by
-
Structure, function, and lipid sensing activity in the thioesterase superfamily.Biochem Soc Trans. 2024 Aug 28;52(4):1565-1577. doi: 10.1042/BST20230313. Biochem Soc Trans. 2024. PMID: 39140379 Free PMC article. Review.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources