INTRACELLULAR-LOCALIZATION OF HEPATIC PROPIONYL-COA CARBOXYLASE AND METHYLMALONYL-COA MUTASE IN HUMANS AND NORMAL AND VITAMIN-B12 DEFICIENT RATS
INTRACELLULAR-LOCALIZATION OF HEPATIC PROPIONYL-COA CARBOXYLASE AND METHYLMALONYL-COA MUTASE IN HUMANS AND NORMAL AND VITAMIN-B12 DEFICIENT RATS
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DOI：
10.1111/j.1365-2141.1975.tb00885.x
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发表时间：
1975-01-01
影响因子：
6.5
通讯作者：
KITCHENS, RL
中科院分区：
文献类型：
--
作者：
FRENKEL, EP;KITCHENS, RL
摘要在取自正常和维生素 B12 缺乏的大鼠以及人类的大鼠肝脏中，研究了涉及丙酸氧化的维生素 B12 依赖性途径中酶的细胞内定位。测定了丙酰辅酶 A 羧化酶和维生素 B12 依赖性甲基丙二酰辅酶 A 变位酶的亚细胞位点。这两种酶的所有活性都被证明位于线粒体中，并且这些酶被证明与线粒体的内膜基质部分松散结合。维生素 B12 缺乏不会改变亚细胞定位。最后，描述了甲基丙二酰辅酶A变位酶的快速酶测定。
SummaryThe intracellular localization of the enzymes in the vitamin B12dependent pathway which involves the oxidation of propionate was studied in rat liver obtained from normal and vitamin B12deficient rats as well as from man. The subcellular site of propionyl CoA carboxylase and the vitamin B12dependent‐methylmalonyl CoA mutase were determined. All of the activity of these two enzymes was demonstrated to be in the mitochondria and those enzymes were shown to be loosely bound to the inner membrane‐matrix portion of the mitochondria. Vitamin B12deficiency did not alter the subcellular localization. Finally, a rapid enzymatic assay for methylmalonyl‐CoA mutase was described.