Expression of Functional Human Monoamine Oxidase A and B cDNAs in Mammalian Cells
Expression of Functional Human Monoamine Oxidase A and B cDNAs in Mammalian Cells
复制标题
功能性人单胺氧化酶 A 和 B cDNA 在哺乳动物细胞中的表达
作者：
N. Lan;Chonghong Chen;J. Shih
摘要：单胺氧化酶A和单胺氧化酶B是代谢生物胺的重要酶。先前的研究表明，MAO A和MAO B分别由两个亚基组成，分子量分别为63和60千道尔顿。编码人肝脏MAO A和B亚基的cdna已通过转染单个克隆在哺乳动物细胞中表达。由这些cdna表达的蛋白质被证明具有催化活性。与内源性酶相似，表达的MAO A倾向于将5 -羟色胺作为底物，并且对抑制剂clorgyline敏感。相比之下，表达的MAO B倾向于苯乙基胺作为底物，并且对抑制剂去戊烯基敏感。这些结果表明MAO a（或B）的单个多肽，以单体或二聚体的形式存在，具有酶活性。从各自的cDNA克隆中获得功能性MAO A和B的能力使我们能够进一步研究这些重要酶的结构和功能关系。
Abstract: Monoamine oxidase (MAO) A and B are important enzymes that metabolize biogenic amines throughout the body. Previous studies had suggested that both MAO A and B consist of two subunits of molecular masses of 63 and 60 kilodaltons, respectively. The cDNAs encoding one subunit of human liver MAO A and B have been expressed in mammalian cells by transfection of the individual clones. The proteins expressed from these cDNAs are shown to be catalytically active. Similar to the endogenous enzymes, the expressed MAO A prefers serotonin as a substrate and is sensitive to the inhibitor clorgyline. In contrast, the expressed MAO B prefers phenylethyl‐amine as a substrate and is sensitive to the inhibitor deprenyl. These results suggest that a single polypeptide of MAO A (or B), existing as either a monomer or homodimer, is enzymatically active. The ability to obtain functional MAO A and B from their respective cDNA clones allows us to study further the structure and function relationships of these important enzymes.
4-氟-3-硝基苯基叠氮对人胎盘单胺氧化酶-A 进行光亲和标记。
影响因子：
3.6
作者：
Hsu,MC;Shih,JC
通讯作者：
Shih,JC
DOI：
10.1073/pnas.85.13.4934
发表时间：
1988-07-01
影响因子：
11.1
作者：
BACH, AWJ;LAN, NC;SHIH, JC
通讯作者：
SHIH, JC
人“A”型和牛“B”型单胺氧化酶活性位点黄素肽片段的身份。
影响因子：
3.9
作者：
Nagy,J;Salach,JI
通讯作者：
Salach,JI