Identity of the active site flavin-peptide fragments from the human "A"-form and the bovine "B"-form of monoamine oxidase.
Identity of the active site flavin-peptide fragments from the human "A"-form and the bovine "B"-form of monoamine oxidase.
复制标题
人“A”型和牛“B”型单胺氧化酶活性位点黄素肽片段的身份。
DOI：
10.1016/0003-9861(81)90523-3
复制
发表时间：
1981
影响因子：
3.9
通讯作者：
Salach,JI
中科院分区：
文献类型：
--
作者：
Nagy,J;Salach,JI
证实人胎盘线粒体中存在的单胺氧化酶为氯碱敏感型或A型。经过广泛的磷脂酶处理和Triton X-100萃取后，这一特性并没有消失。利用胰蛋白酶和凝乳胰蛋白酶对部分纯化的酶进行蛋白水解消化，并分离出含有共价连接的黄素辅酶的肽，从而可以测定酶的催化位点的黄素区域的氨基酸组成和序列。黄素肽的结构被发现与牛肝酶的结构相同，而牛肝酶对氯绿碱不敏感，因此是B型。线粒体单胺氧化酶的黄素肽片段因此在两种形式之间和哺乳动物物种之间是保守的。
The monoamine oxidase present in the mitochondria of human placenta was verified to be the clorygyline sensitive or A form. This property was not abolished following extensive phospholipase treatment and Triton X-100 extraction. Proteolytic digestion of the partially purified enzyme using trypsin and chymotrypsin and isolation of a peptide containing the covalently linked flavin coenzyme permitted determination of the amino acid composition and sequence of the flavin region of the catalytic site of the enzyme. The structure of the flavin peptide was found to be identical to that of the bovine liver enzyme which is clorgyline insensitive, hence, the B form. The flavin peptide segment of mitochondrial monoamine oxidase is thus conserved between the two forms and among mammalian species.