{"title":"γ-羟谷氨酸在大鼠肝脏中的代谢ⅱ。一种与γ-羟谷氨酸代谢有关的转氨酶","authors":"Kazuoki Kuratomi, Keiko Fukunaga, Yasuko Kobayashi","doi":"10.1016/0006-3002(63)91028-X","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. An enzyme which catalyses the transamination between γ-hydroxyglutamate and α-ketoglutarate was extracted from rat-liver acetone powder and purified in excess of 15-fold. Fractionation of the enzyme from a separate aspartate transaminase (<span>L</span>-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1) remained incomplete.</p></span></li><li><span>2.</span><span><p>2. [2-<sup>14</sup>C]Pyruvate was incorporated into γ-hydroxy-α-ketoglutarate and γ-hydroxyglutamate in the presence of glyoxylate in rat-liver homogenate. Specific activity values of these three compounds indicated the occurence of the following pathway: Pyruvate + glyoxylate ⇌ γ-hydroxy-α-ketoglutarate ⇌ γ-hydroxyglutamate.</p></span></li><li><span>3.</span><span><p>3. A further possible pathway of γ-hydroxy-α-ketoglutarate metabolism leading to malate and of γ-hydroxyglutamate to its decarboxylation product or to <span>L</span>-hydroxyproline were inferred and discussed.</p></span></li></ul></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91028-X","citationCount":"8","resultStr":"{\"title\":\"The metabolism of γ-hydroxyglutamate in rat liver II. A transaminase concerned in γ-hydroxyglutamate metabolism\",\"authors\":\"Kazuoki Kuratomi, Keiko Fukunaga, Yasuko Kobayashi\",\"doi\":\"10.1016/0006-3002(63)91028-X\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. An enzyme which catalyses the transamination between γ-hydroxyglutamate and α-ketoglutarate was extracted from rat-liver acetone powder and purified in excess of 15-fold. Fractionation of the enzyme from a separate aspartate transaminase (<span>L</span>-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1) remained incomplete.</p></span></li><li><span>2.</span><span><p>2. [2-<sup>14</sup>C]Pyruvate was incorporated into γ-hydroxy-α-ketoglutarate and γ-hydroxyglutamate in the presence of glyoxylate in rat-liver homogenate. Specific activity values of these three compounds indicated the occurence of the following pathway: Pyruvate + glyoxylate ⇌ γ-hydroxy-α-ketoglutarate ⇌ γ-hydroxyglutamate.</p></span></li><li><span>3.</span><span><p>3. A further possible pathway of γ-hydroxy-α-ketoglutarate metabolism leading to malate and of γ-hydroxyglutamate to its decarboxylation product or to <span>L</span>-hydroxyproline were inferred and discussed.</p></span></li></ul></div>\",\"PeriodicalId\":94301,\"journal\":{\"name\":\"Biochimica et biophysica acta\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1963-12-13\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0006-3002(63)91028-X\",\"citationCount\":\"8\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et biophysica acta\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/000630026391028X\",\"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","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/000630026391028X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The metabolism of γ-hydroxyglutamate in rat liver II. A transaminase concerned in γ-hydroxyglutamate metabolism
1.
1. An enzyme which catalyses the transamination between γ-hydroxyglutamate and α-ketoglutarate was extracted from rat-liver acetone powder and purified in excess of 15-fold. Fractionation of the enzyme from a separate aspartate transaminase (L-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1) remained incomplete.
2.
2. [2-14C]Pyruvate was incorporated into γ-hydroxy-α-ketoglutarate and γ-hydroxyglutamate in the presence of glyoxylate in rat-liver homogenate. Specific activity values of these three compounds indicated the occurence of the following pathway: Pyruvate + glyoxylate ⇌ γ-hydroxy-α-ketoglutarate ⇌ γ-hydroxyglutamate.
3.
3. A further possible pathway of γ-hydroxy-α-ketoglutarate metabolism leading to malate and of γ-hydroxyglutamate to its decarboxylation product or to L-hydroxyproline were inferred and discussed.
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