IDENTIFICATION OF FOLATE BINDING-PROTEIN OF MITOCHONDRIA AS DIMETHYLGLYCINE DEHYDROGENASE
IDENTIFICATION OF FOLATE BINDING-PROTEIN OF MITOCHONDRIA AS DIMETHYLGLYCINE DEHYDROGENASE
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DOI：
10.1073/pnas.77.8.4484
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发表时间：
1980-01-01
期刊：
影响因子：
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通讯作者：
WAGNER, C
中科院分区：
文献类型：
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作者：
WITTWER, AJ;WAGNER, C
采用凝胶过滤、DEAE-纤维素和亲和层析相结合的方法纯化了大鼠肝线粒体叶酸结合蛋白。该蛋白通过其在体外结合四氢[3 H]叶酸的能力进行测定。纯化的蛋白质含有紧密结合的黄素，通过十二烷基硫酸钠电泳测定其分子量约为90，000。该蛋白质显示二甲基甘氨酸脱氢酶[EC 1.5.99.2]活性，其与叶酸结合活性共纯化。四氢叶酸的作用可能是接受反应过程中产生的甲醛。
The folate-binding protein of rat liver mitochondria was purified to homogeneity by a combination of gel filtration, DEAE-cellulose and affinity chromatography. This protein was assayed by its ability to bind tetrahydro[3H]folic acid in vitro. The purified protein contains tightly bound flavin and has a MW of about 90,000 as determined by sodium dodecyl sulfate electrophoresis. This protein displays dimethylglycine dehydrogenase, [EC 1.5.99.2] activity which copurifies with the folate-binding activity. The role of the tetrahydrofolic acid may be to accept the formaldehyde produced during the course of the reaction.