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Effects of pH on horse liver aldehyde dehydrogenase: alterations in metal ion activation, number of functioning active sites, and hydrolysis of the acyl intermediate.
Takahashi K, Weiner H, Filmer DL. Takahashi K, et al. Among authors: weiner h. Biochemistry. 1981 Oct 13;20(21):6225-30. doi: 10.1021/bi00524a049. Biochemistry. 1981. PMID: 7306510
The Mg2+ ion activation of the steady-state velocity at pH 7.5 has been explained through a mechanism involving alteration of the tetrameric enzyme, functioning with half-of-the-sites reactivity, to a dimeric enzyme, functioning with all-of-the-sites reactivity [Takahashi, K., &a …
The Mg2+ ion activation of the steady-state velocity at pH 7.5 has been explained through a mechanism involving alteration of the tetrameric …
Nicotinamide adenine dinucleotide activation of the esterase reaction of horse liver aldehyde dehydrogenase.
Takahashi K, Weiner H. Takahashi K, et al. Among authors: weiner h. Biochemistry. 1981 May 12;20(10):2720-6. doi: 10.1021/bi00513a003. Biochemistry. 1981. PMID: 7248246
Mg2+ ions activate the dehydrogenase reaction of horse liver aldehyde dehydrogenase (Takahashi, K., & Weiner, H. (1980) J. Biol. Chem. 255, 8206-8209). The metal neither increased the esterase reaction nor affected the NAD activation. The rate-limiting step for …
Mg2+ ions activate the dehydrogenase reaction of horse liver aldehyde dehydrogenase (Takahashi, K., & Weiner, H. (1980) J. …
1,335 results