{"title":"线粒体中的蛋白质合成","authors":"A.M. Kroon","doi":"10.1016/0926-6550(64)90178-1","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. A procedure for preparing rat-liver mitochondria including a pre-incubation with RNAase (EC 2.7.7.16) to inactivate the microsomal system for amino acid incorporation is described.</p></span></li><li><span>2.</span><span><p>2. The inhibition of the incorporation of amino acids into mitochondrial protein by adding substrate is correlated with a lowering of the NADP<sup>+</sup>/NADPH ratio.</p></span></li><li><span>3.</span><span><p>3. It is shown that ammonia can relieve the inhibition by α-oxoglutarate or isocitrate of the incorporation into liver mitochondria, that this effect is not due to the glutamate formed, and that this is correlated with oxidation of NADPH to NADP<sup>+</sup>.</p></span></li><li><span>4.</span><span><p>4. The role of endogenous substrate is discussed. It is concluded that in the case of rat-liver mitochondria α-oxoglutarate plus ammonia give the best conditions for providing energy for incorporation, since a high NADP<sup>+</sup>/NADPH ratio is also assured.</p></span></li><li><span>5.</span><span><p>5. Judged by the effects of oligomycin and 2,4-dinitrophenol on the amino acid incorporation into protein by mitochondria, the possibility is discussed whether and in how far the high-energy intermediates of oxidative phosphorylation can meet the energy requirements for the incorporation process.</p></span></li></ul></div>","PeriodicalId":100173,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1964-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6550(64)90178-1","citationCount":"36","resultStr":"{\"title\":\"Protein synthesis in mitochondria\",\"authors\":\"A.M. Kroon\",\"doi\":\"10.1016/0926-6550(64)90178-1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. A procedure for preparing rat-liver mitochondria including a pre-incubation with RNAase (EC 2.7.7.16) to inactivate the microsomal system for amino acid incorporation is described.</p></span></li><li><span>2.</span><span><p>2. The inhibition of the incorporation of amino acids into mitochondrial protein by adding substrate is correlated with a lowering of the NADP<sup>+</sup>/NADPH ratio.</p></span></li><li><span>3.</span><span><p>3. It is shown that ammonia can relieve the inhibition by α-oxoglutarate or isocitrate of the incorporation into liver mitochondria, that this effect is not due to the glutamate formed, and that this is correlated with oxidation of NADPH to NADP<sup>+</sup>.</p></span></li><li><span>4.</span><span><p>4. The role of endogenous substrate is discussed. It is concluded that in the case of rat-liver mitochondria α-oxoglutarate plus ammonia give the best conditions for providing energy for incorporation, since a high NADP<sup>+</sup>/NADPH ratio is also assured.</p></span></li><li><span>5.</span><span><p>5. Judged by the effects of oligomycin and 2,4-dinitrophenol on the amino acid incorporation into protein by mitochondria, the possibility is discussed whether and in how far the high-energy intermediates of oxidative phosphorylation can meet the energy requirements for the incorporation process.</p></span></li></ul></div>\",\"PeriodicalId\":100173,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-09-11\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6550(64)90178-1\",\"citationCount\":\"36\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926655064901781\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926655064901781","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
1. A procedure for preparing rat-liver mitochondria including a pre-incubation with RNAase (EC 2.7.7.16) to inactivate the microsomal system for amino acid incorporation is described.
2.
2. The inhibition of the incorporation of amino acids into mitochondrial protein by adding substrate is correlated with a lowering of the NADP+/NADPH ratio.
3.
3. It is shown that ammonia can relieve the inhibition by α-oxoglutarate or isocitrate of the incorporation into liver mitochondria, that this effect is not due to the glutamate formed, and that this is correlated with oxidation of NADPH to NADP+.
4.
4. The role of endogenous substrate is discussed. It is concluded that in the case of rat-liver mitochondria α-oxoglutarate plus ammonia give the best conditions for providing energy for incorporation, since a high NADP+/NADPH ratio is also assured.
5.
5. Judged by the effects of oligomycin and 2,4-dinitrophenol on the amino acid incorporation into protein by mitochondria, the possibility is discussed whether and in how far the high-energy intermediates of oxidative phosphorylation can meet the energy requirements for the incorporation process.
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