铁限制生长对产朊假丝酵母线粒体中还原型烟酰胺腺嘌呤二核苷酸脱氢酶活性及膜蛋白的影响。
The effects of iron-limited growth on the reduced nicotinamide-adenine dinucleotide dehydrogenase activity and the membrane proteins of Candida utilis mitochondria.
作者信息
Clegg R A, Skyrme J E
出版信息
Biochem J. 1973 Dec;136(4):1029-37. doi: 10.1042/bj1361029.
Abstract
- The mitochondrial NADH dehydrogenase (EC 1.6.99.3) of Candida utilis exhibited altered properties when the organism was grown under iron-limited conditions. No suitable acceptor was found for assay of this enzyme from iron-limited cells. 2. Mitochondrial membrane proteins from C. utilis were analysed by polyacrylamide-gel electrophoresis. Compared with glycerol-limited cells, iron limitation resulted in the loss of at least two polypeptides from the mitochondrial membrane. 3. Neither of the polypeptides affected by iron limitation was part of a cytochrome, although one of them was part of the mitochondrial NADH dehydrogenase. 4. Non-haem iron of mitochondrial membranes was released in the presence of sodium dodecyl sulphate, and electrophoresis in solutions of this detergent cannot be used directly to identify iron-sulphur proteins. Non-ionic detergents do not release non-haem iron but nor do they provide a satisfactory system for electrophoretic separation.
摘要
- 当产朊假丝酵母在铁限制条件下生长时，其线粒体NADH脱氢酶（EC 1.6.99.3）表现出性质改变。未找到合适的受体用于测定来自铁限制细胞的这种酶。2. 用聚丙烯酰胺凝胶电泳分析了产朊假丝酵母的线粒体膜蛋白。与甘油限制细胞相比，铁限制导致线粒体膜中至少两种多肽缺失。3. 受铁限制影响的两种多肽都不是细胞色素的一部分，尽管其中一种是线粒体NADH脱氢酶的一部分。4. 线粒体膜的非血红素铁在十二烷基硫酸钠存在下会释放出来，并且在这种去污剂溶液中的电泳不能直接用于鉴定铁硫蛋白。非离子去污剂不会释放非血红素铁，但它们也不能提供令人满意的电泳分离系统。
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The effects of iron-limited growth on the reduced nicotinamide-adenine dinucleotide dehydrogenase activity and the membrane proteins of Candida utilis mitochondria.铁限制生长对产朊假丝酵母线粒体中还原型烟酰胺腺嘌呤二核苷酸脱氢酶活性及膜蛋白的影响。
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本文引用的文献
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Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
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NITRATE REDUCTASE IN CELL-FREE EXTRACTS OF A HAEMIN-REQUIRING STRAIN OF STAPHYLOCOCCUS AUREUS.一株需要血红素的金黄色葡萄球菌无细胞提取物中的硝酸还原酶
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FEBS Lett. 1969 Nov 12;5(3):207-210. doi: 10.1016/0014-5793(69)80333-9.
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The oxidation-reduction potentials of iron-sulfur centers in the site I region of the respiratory chain in C. utilis submitochondrial particles.
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Iron-limited growth of torulopsis utilis, and the reversible loss of mitochondrial energy conservation at site 1 and of sensitivity to rotenone and piericidin A.
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