Zinc in horse liver alcohol dehvdrogenase.
نویسندگان
چکیده
The alcohol dehydrogenase (ADH’) of yeast has twice the molecular weight of the ADH of horse liver (l), contains 4 gm. atoms of zinc (2), and binds 4 moles of DPN per mole of protein (1). The liver ADH binds 2 moles of coenzyme per mole (3). These facts prompted the prediction that the liver ADH should contain 2 gm. atoms of zinc per mole of protein (2). The presence of 2 atoms of zinc in liver ADH has been briefly reported (4,5). This paper presents detailed spectrographic, microchemical, and polarographic analyses which demonstrate the presence of 2 atoms of zinc per molecule of liver ADH; all other metals are removed during purification. The activity of the enzyme can be modified in a manner analogous to but not identical with that observed for other zinc dehydrogenases.
منابع مشابه
The nature of binding of competitive inhibitors to alcohol dehydrogenases.
Two classes of metal ion binding sites in horse liver alcohol dehydrogenase are distinguished by the observed rates of replacement of zinc by cobalt in acetate and in Z-(N-morpholine)-ethane sulfonic acid buffers. Hybrid enzymes containing both zinc and cobalt metal ions have been prepared and exhibit visible absorption maxima at 655 nm and 740 nm. Binding of azide, a substrate-competitive inhi...
متن کاملThe role of zinc in alcohol dehydrogenase. IV. The kinetics of the instantaneous inhibition of horse liver alcohol dehydrogenase by 1,10-phenanthroline.
The alcohol dehydrogenase crystallized from horse liver contains 2 atoms of zinc per molecule and the activity of this enzyme is inhibited by metal-binding agents (1, 2). The inhibition of liver alcohol dehydrogenase by one of these agents, 1, IO-phenanthroline, differs from that which is observed when the alcohol dehydrogenase isolated from yeast is exposed to 1, lo-phenanthroline (3). The liv...
متن کاملThe Role of Zinc in Alcohol Dehydrogenase IV. THE KIh’ETICS OF THE INSTANTANEOUS INHIBITION OF HORSE LIVER ALCOHOL DEHYDROGENASE BY 1 , lo-PHENANTHROLINE*
The alcohol dehydrogenase crystallized from horse liver contains 2 atoms of zinc per molecule and the activity of this enzyme is inhibited by metal-binding agents (1, 2). The inhibition of liver alcohol dehydrogenase by one of these agents, 1, IO-phenanthroline, differs from that which is observed when the alcohol dehydrogenase isolated from yeast is exposed to 1, lo-phenanthroline (3). The liv...
متن کاملZinc in Horse Liver Alcohol Dehydrogenase* by Bert L. Vallee
The alcohol dehydrogenase (ADH’) of yeast has twice the molecular weight of the ADH of horse liver (l), contains 4 gm. atoms of zinc (2), and binds 4 moles of DPN per mole of protein (1). The liver ADH binds 2 moles of coenzyme per mole (3). These facts prompted the prediction that the liver ADH should contain 2 gm. atoms of zinc per mole of protein (2). The presence of 2 atoms of zinc in liver...
متن کاملThe interaction of triiodothyroacetic acid with horse liver alcohol dehydrogenase.
Triiodothyroacetic acid is a competitive inhibitor of horse liver alcohol dehydrogenase with respect to the coenzyme. The Ki value for triiodothyroacetic acid in this system is 1.3 to 1.9 AuM. Triiodothyroacetic acid appears to interact with a hydrophobic portion of the protein since it is able to displace the hydrophobic compound, 8-anilino1 -naphthalene sulfonic acid from liver alcohol dehydr...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 225 1 شماره
صفحات -
تاریخ انتشار 1957