{"title":"面包酵母鸟苷酸激酶的纯化及性质研究","authors":"Mitsuaki Moriguchi, Hirao Kohno, Masaharu Kamei, Tatsurokuro Tochikura","doi":"10.1016/0005-2744(81)90239-4","DOIUrl":null,"url":null,"abstract":"<div><p>Guanylate kinase (ATP:(d)GMP phosphotransferase, EC 2.7.4.8) was purified about 200-fold with 4% yield from baker's yeast. The enzyme preparation showed a single band on polyacrylamide gel electrophoresis and the molecular weight of the enzyme was calculated to be 25 000 by gel filtration. With ATP as a phosphate donor, the kinase used only GMP as a phosphate acceptor. <span><math><mtext>K</mtext><msub><mi></mi><mn><mtext>m</mtext></mn></msub></math></span> values for ATP and GMP were 0.5 and 0.048 mM, respectively. The enzyme reacted optimally at pH 7.5. The enzyme was labile during storage at 4°C and inactivation was prevented by 20% glycerol.</p></div>","PeriodicalId":100159,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology","volume":"662 1","pages":"Pages 165-167"},"PeriodicalIF":0.0000,"publicationDate":"1981-11-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2744(81)90239-4","citationCount":"8","resultStr":"{\"title\":\"Purification and properties of guanylate kinase from baker's yeast\",\"authors\":\"Mitsuaki Moriguchi, Hirao Kohno, Masaharu Kamei, Tatsurokuro Tochikura\",\"doi\":\"10.1016/0005-2744(81)90239-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Guanylate kinase (ATP:(d)GMP phosphotransferase, EC 2.7.4.8) was purified about 200-fold with 4% yield from baker's yeast. The enzyme preparation showed a single band on polyacrylamide gel electrophoresis and the molecular weight of the enzyme was calculated to be 25 000 by gel filtration. With ATP as a phosphate donor, the kinase used only GMP as a phosphate acceptor. <span><math><mtext>K</mtext><msub><mi></mi><mn><mtext>m</mtext></mn></msub></math></span> values for ATP and GMP were 0.5 and 0.048 mM, respectively. The enzyme reacted optimally at pH 7.5. The enzyme was labile during storage at 4°C and inactivation was prevented by 20% glycerol.</p></div>\",\"PeriodicalId\":100159,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Enzymology\",\"volume\":\"662 1\",\"pages\":\"Pages 165-167\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1981-11-13\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0005-2744(81)90239-4\",\"citationCount\":\"8\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Enzymology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0005274481902394\",\"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) - Enzymology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005274481902394","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Purification and properties of guanylate kinase from baker's yeast
Guanylate kinase (ATP:(d)GMP phosphotransferase, EC 2.7.4.8) was purified about 200-fold with 4% yield from baker's yeast. The enzyme preparation showed a single band on polyacrylamide gel electrophoresis and the molecular weight of the enzyme was calculated to be 25 000 by gel filtration. With ATP as a phosphate donor, the kinase used only GMP as a phosphate acceptor. values for ATP and GMP were 0.5 and 0.048 mM, respectively. The enzyme reacted optimally at pH 7.5. The enzyme was labile during storage at 4°C and inactivation was prevented by 20% glycerol.
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