Chromosome assignment, biochemical and immunological studies on a human aldehyde dehydrogenase, ALDH3
Chromosome assignment, biochemical and immunological studies on a human aldehyde dehydrogenase, ALDH3
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人乙醛脱氢酶 ALDH3 的染色体分配、生化和免疫学研究
DOI：
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发表时间：
1985
影响因子：
1.9
通讯作者：
D. Hopkinson
中科院分区：
文献类型：
--
作者：
I. Santisteban;S. Povey;L. West;J. Parrington;D. Hopkinson
已在人体组织中检查了 ALDH 同工酶的生化特性，并对一组称为 ALDH3 的同工酶进行了详细研究。这些成分在肺和胃中含量最高，但在胎儿组织、血液、毛根和成纤维细胞中不表达。 ALDH3 同工酶对苯甲醛表现出最佳活性，并且可以使用 NAD 或 NADP 作为辅因子。来自胃的部分纯化的 ALDH3 抗血清选择性地从人体组织中沉淀出该同工酶，并选择性地识别大鼠体内的同源成分。人类和啮齿动物 ALDH3 不会被抗 ALDH1 或抗 ALDH2 抗血清免疫沉淀。在使用大鼠肝癌细胞构建的人类与啮齿动物杂交体中发现了高水平的表达，这些杂交体用于将人类 ALDH3 基因分配到 17 号染色体。
The biochemical properties of ALDH isozymes have been examined in human tissues and one set, designated ALDH3, has been studied in detail. These components occur at highest levels in lung and stomach, but were not expressed in fetal tissues, or in blood, hair roots and fibroblasts. The ALDH3 isozymes show optimal activity with benzaldehyde and can use either NAD or NADP as cofactor. Antiserum against a partially purified ALDH3, from stomach, selectively precipitates this isozyme from human tissues and selectively recognizes an homologous component in the rat. Human and rodent ALDH3 were not immunoprecipitated by anti‐ALDH1 or anti‐ALDH2 antisera. High levels of expression were found in human‐rodent hybrids, constructed using rat hepatoma cells, and these hybrids were used to assign the human ALDH3 gene to chromosome 17.
人肝乙醇脱氢酶：β2β2东方同工酶中的氨基酸取代解释了功能特性，建立了活性位点结构，并与酵母酶中的突变交换相似。
DOI：
10.1073/pnas.81.10.3024
发表时间：
1984
影响因子：
11.1
作者：
Jörnvall,H;Hempel,J;Vallee,BL;Bosron,WF;Li,TK
通讯作者：
Li,TK
人乙醇脱氢酶的分子遗传学分析。
DOI：
10.1016/0741-8329(85)90015-1
发表时间：
1985
期刊：
Alcohol (Fayetteville, N.Y.)
影响因子：
--
作者：
Duester,G;Hatfield,GW;Smith,M
通讯作者：
Smith,M