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Zinc isotope exchange in horse liver alcohol dehydrogenase.

作者信息

Drum D E, Li T K, Vallee B L

出版信息

Biochemistry. 1969 Sep;8(9):3792-7. doi: 10.1021/bi00837a045.

DOI:10.1021/bi00837a045
PMID:5387530
Abstract
摘要

相似文献

1
Zinc isotope exchange in horse liver alcohol dehydrogenase.马肝醇脱氢酶中的锌同位素交换
Biochemistry. 1969 Sep;8(9):3792-7. doi: 10.1021/bi00837a045.
2
Considerations in evaluating the zinc content of horse liver alcohol dehydrogenase preparations.
Biochemistry. 1969 Sep;8(9):3783-91. doi: 10.1021/bi00837a044.
3
Interaction of coenzyme with differently prepared zinc-free (apo) horse liver alcohol dehydrogenases.
J Biol Chem. 1969 Nov 10;244(21):5967-71.
4
THE EFFECTS OF COENZYMES AND SUBSTRATES ON THE RATE OF ZINC EXCHANGE IN HORSE LIVER ALCOHOL DEHYDROGENASE.辅酶和底物对马肝醇脱氢酶中锌交换速率的影响。
Biochemistry. 1964 Jul;3:944-9. doi: 10.1021/bi00895a017.
5
Function of zinc in horse liver alcohol dehydrogenase.锌在马肝乙醇脱氢酶中的作用。
Arch Biochem Biophys. 1967 Mar;119(1):552-9. doi: 10.1016/0003-9861(67)90490-0.
6
Effect of various environments on the intrinsic fluorescence polarization spectra of horse liver alcohol dehydrogenase.
Arch Biochem Biophys. 1969 Dec;135(1):218-30. doi: 10.1016/0003-9861(69)90533-5.
7
Enhancement of the activity of horse liver alcohol dehydrogenase by modification of amino groups at the active sites.通过修饰活性位点的氨基来增强马肝醇脱氢酶的活性。
J Biol Chem. 1970 Apr 10;245(7):1727-35.
8
35 C1 NMR studies of the active site zinc of horse liver alcohol dehydrogenase.马肝醇脱氢酶活性位点锌的35 C1核磁共振研究。
Biochem Biophys Res Commun. 1971 Dec 17;45(6):1444-50. doi: 10.1016/0006-291x(71)90182-3.
9
Roles of zinc ion and reduced coenzyme in the formation of a transient chemical intermediate during the equine liver alcohol dehydrogenase catalyzed reduction of an aromatic aldehyde.锌离子和还原型辅酶在马肝乙醇脱氢酶催化芳香醛还原过程中形成瞬态化学中间体的作用。
Biochemistry. 1973 Nov 20;12(24):4882-92. doi: 10.1021/bi00748a012.
10
Heterogeneity in the rapidly exchanging metals of horse liver alcohol dehydrogenase.马肝醇脱氢酶快速交换金属中的异质性。
Biochem Biophys Res Commun. 1975 Oct 6;66(3):935-41. doi: 10.1016/0006-291x(75)90730-5.

引用本文的文献

1
Coordination dynamics of biological zinc "clusters" in metallothioneins and in the DNA-binding domain of the transcription factor Gal4.金属硫蛋白和转录因子Gal4的DNA结合结构域中生物锌“簇”的配位动力学
Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2233-7. doi: 10.1073/pnas.94.6.2233.
2
The presence and possible role of zinc in RNA polymerase obtained from Escherichia coli.锌在从大肠杆菌中获得的RNA聚合酶中的存在及可能作用。
Proc Natl Acad Sci U S A. 1971 Oct;68(10):2497-501. doi: 10.1073/pnas.68.10.2497.
3
Partial similarities between yeast and liver alcohol dehydrogenases.
酵母乙醇脱氢酶与肝脏乙醇脱氢酶之间的部分相似性。
Proc Natl Acad Sci U S A. 1973 Aug;70(8):2295-8. doi: 10.1073/pnas.70.8.2295.
4
Structure of liver alcohol dehydrogenase at 2.9-angstrom resolution.分辨率为 2.9 埃的肝脏乙醇脱氢酶结构。
Proc Natl Acad Sci U S A. 1973 Aug;70(8):2439-42. doi: 10.1073/pnas.70.8.2439.
5
Rat liver alcohol dehydrogenase. Purification and properties.大鼠肝脏乙醇脱氢酶。纯化及性质
Biochem J. 1971 Dec;125(4):1039-47. doi: 10.1042/bj1251039.
6
Chemical reactivities of catalytic and noncatalytic zinc or cobalt atoms of horse liver alcohol dehydrogenase: differentiation by their thermodynamic and kinetic properties.马肝醇脱氢酶催化和非催化锌或钴原子的化学反应性：通过其热力学和动力学性质进行区分
Proc Natl Acad Sci U S A. 1976 Feb;73(2):344-8. doi: 10.1073/pnas.73.2.344.