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The catalytic metal atoms of cobalt substituted liver alcohol dehydrogenase.

作者信息

Sytkowski A J, Vallee B L

出版信息

Biochem Biophys Res Commun. 1975 Dec 15;67(4):1488-93. doi: 10.1016/0006-291x(75)90194-1.

DOI:10.1016/0006-291x(75)90194-1
PMID:1239290
Abstract
摘要

相似文献

1
The catalytic metal atoms of cobalt substituted liver alcohol dehydrogenase.钴取代的肝脏乙醇脱氢酶的催化金属原子。
Biochem Biophys Res Commun. 1975 Dec 15;67(4):1488-93. doi: 10.1016/0006-291x(75)90194-1.
2
Metal-directed affinity labeling of zinc(II), cobalt(II), and cadmium(II) horse liver alcohol dehydrogenases.锌(II)、钴(II)和镉(II)马肝醇脱氢酶的金属导向亲和标记
J Inorg Biochem. 1981 Aug;15(1):79-87. doi: 10.1016/s0162-0134(00)80137-3.
3
Site-specific substituted cobalt(II) horse liver alcohol dehydrogenases. Preparation and characterization in solution, crystalline and immobilized state.
Eur J Biochem. 1979 Aug 1;98(2):501-12. doi: 10.1111/j.1432-1033.1979.tb13211.x.
4
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.
5
The role of metal in liver alcohol dehydrogenase catalysis. Spectral and kinetic studies with cobalt-substituted enzyme.金属在肝脏乙醇脱氢酶催化中的作用。钴取代酶的光谱和动力学研究。
J Biol Chem. 1975 Mar 25;250(6):2008-12.
6
Liver alcohol dehydrogenase: evidence for a new cobalt/zinc hybrid.肝脏乙醇脱氢酶:一种新型钴/锌杂合物的证据。
Biochem Biophys Res Commun. 1976 Oct 4;72(3):886-92. doi: 10.1016/s0006-291x(76)80215-x.
7
Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 1. Copper(II) and cobalt(II) ions.
Biochemistry. 1981 Jun 9;20(12):3424-32. doi: 10.1021/bi00515a019.
8
Cobalt exchange in horse liver alcohol dehydrogenase.马肝醇脱氢酶中的钴交换
Biochemistry. 1978 Jul 11;17(14):2850-7. doi: 10.1021/bi00607a024.
9
Kinetics and mechanisms of the recombination of Zn2+, Co2+, and Ni2+ with the metal-depleted catalytic site of horse liver alcohol dehydrogenase.锌离子、钴离子和镍离子与马肝醇脱氢酶金属缺失催化位点重组的动力学及机制
J Inorg Biochem. 1983 Feb;18(1):59-69. doi: 10.1016/0162-0134(83)85040-5.
10
Estimate of minimal distance between rapidly exchanging zinc and nucleotide binding sites in liver alcohol dehydrogenase.肝脏乙醇脱氢酶中快速交换的锌离子与核苷酸结合位点之间最小距离的估计
Biochemistry. 1973 Nov 6;12(23):4743-50. doi: 10.1021/bi00747a029.

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1
L-histidine inhibits production of lysophosphatidic acid by the tumor-associated cytokine, autotaxin.L-组氨酸可抑制肿瘤相关细胞因子自分泌运动因子产生溶血磷脂酸。
Lipids Health Dis. 2005 Feb 28;4:5. doi: 10.1186/1476-511X-4-5.
2
The role of metals in carcinogenesis: biochemistry and metabolism.金属在致癌作用中的角色:生物化学与代谢
Environ Health Perspect. 1981 Aug;40:233-52. doi: 10.1289/ehp.8140233.
3
Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivatives.
特定金属缺失和钴取代的马肝醇脱氢酶衍生物活性位点的晶体结构。
Proc Natl Acad Sci U S A. 1983 Sep;80(17):5289-93. doi: 10.1073/pnas.80.17.5289.