{"title":"小麦胚芽中赖氨酸和蛋氨酸可溶性核糖核酸合成酶的纯化及其性质","authors":"Esam Moustafa","doi":"10.1016/0926-6550(64)90072-6","DOIUrl":null,"url":null,"abstract":"<div><p>Lysyl-s-RNA synthetase (<span>l</span>-lysine: s-RNA ligase (AMP), EC 6.1.1.6) and methionyl-s-RNA-synthetase (<span>l</span>-methionine: s-RNA ligase (AMP), EC 6.1.1.10) were purified from wheat germ about 600-fold and 160-fold, respectively. The two enzymes catalyse amino acid-dependent ATP-pyrophosphate exchange as well as the incorporation of amino acids into s-RNA. The pH optimum of lysine enzyme is in the range 6.8–7.1 and that of methionine enzyme in the range 8.1–8.5. Both enzymes are strongly inhibited by <em>p</em>-hydroxymercuribenzoate and the activity is restored by sulfhydryl group-containing compounds.</p></div>","PeriodicalId":100173,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects","volume":"91 3","pages":"Pages 421-426"},"PeriodicalIF":0.0000,"publicationDate":"1964-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6550(64)90072-6","citationCount":"18","resultStr":"{\"title\":\"Purification and properties of lysyl- and methionyl-soluble ribonucleic acid synthetases from wheat germ\",\"authors\":\"Esam Moustafa\",\"doi\":\"10.1016/0926-6550(64)90072-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Lysyl-s-RNA synthetase (<span>l</span>-lysine: s-RNA ligase (AMP), EC 6.1.1.6) and methionyl-s-RNA-synthetase (<span>l</span>-methionine: s-RNA ligase (AMP), EC 6.1.1.10) were purified from wheat germ about 600-fold and 160-fold, respectively. The two enzymes catalyse amino acid-dependent ATP-pyrophosphate exchange as well as the incorporation of amino acids into s-RNA. The pH optimum of lysine enzyme is in the range 6.8–7.1 and that of methionine enzyme in the range 8.1–8.5. Both enzymes are strongly inhibited by <em>p</em>-hydroxymercuribenzoate and the activity is restored by sulfhydryl group-containing compounds.</p></div>\",\"PeriodicalId\":100173,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects\",\"volume\":\"91 3\",\"pages\":\"Pages 421-426\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-11-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6550(64)90072-6\",\"citationCount\":\"18\",\"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/0926655064900726\",\"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/0926655064900726","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Purification and properties of lysyl- and methionyl-soluble ribonucleic acid synthetases from wheat germ
Lysyl-s-RNA synthetase (l-lysine: s-RNA ligase (AMP), EC 6.1.1.6) and methionyl-s-RNA-synthetase (l-methionine: s-RNA ligase (AMP), EC 6.1.1.10) were purified from wheat germ about 600-fold and 160-fold, respectively. The two enzymes catalyse amino acid-dependent ATP-pyrophosphate exchange as well as the incorporation of amino acids into s-RNA. The pH optimum of lysine enzyme is in the range 6.8–7.1 and that of methionine enzyme in the range 8.1–8.5. Both enzymes are strongly inhibited by p-hydroxymercuribenzoate and the activity is restored by sulfhydryl group-containing compounds.
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