{"title":"d-甘油醛-3-磷酸的副活性:NAD+氧化还原酶(磷酸化)从兔肌肉:NADH-X的形成","authors":"A.G. Hilvers, J.H.M. Weenen, K. Van Dam","doi":"10.1016/0926-6593(66)90143-3","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The formation of NADH-X from NADH in the presence of glyceraldehyde phosphate dehydrogenase (EC 1.2.1.12) at low pH is observed not only in the presence of pyrophosphate, citrate or phosphate, but also in the presence of arsenate.</p></span></li><li><span>2.</span><span><p>2. Stimulation of NADH-X formation by acetyl phosphate is dependent on the presence of enzyme-bound NAD<sup>+</sup>; however, added NAD<sup>+</sup> is inhibitory.</p></span></li><li><span>3.</span><span><p>3. Inhibition of NADH-X formation by sulphydryl reagents is prevented by acetyl phosphate in the presence of pyrophosphate or citrate, but not in the presence of arsenate or phosphate.</p></span></li><li><span>4.</span><span><p>4. In the absence of other polyvalent anions, acetyl phosphate alone can stimulate the conversion of NADH into NADH-X at low pH.</p></span></li><li><span>5.</span><span><p>5. In the presence of acetyl phosphate, the relative rate of formation of NAD<sup>+</sup> and NADH-X from NADH is dependent on the pH and the anions present.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 74-81"},"PeriodicalIF":0.0000,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90143-3","citationCount":"13","resultStr":"{\"title\":\"The side activities of d-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating) from rabbit muscle: NADH-X formation\",\"authors\":\"A.G. Hilvers, J.H.M. Weenen, K. Van Dam\",\"doi\":\"10.1016/0926-6593(66)90143-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. The formation of NADH-X from NADH in the presence of glyceraldehyde phosphate dehydrogenase (EC 1.2.1.12) at low pH is observed not only in the presence of pyrophosphate, citrate or phosphate, but also in the presence of arsenate.</p></span></li><li><span>2.</span><span><p>2. Stimulation of NADH-X formation by acetyl phosphate is dependent on the presence of enzyme-bound NAD<sup>+</sup>; however, added NAD<sup>+</sup> is inhibitory.</p></span></li><li><span>3.</span><span><p>3. Inhibition of NADH-X formation by sulphydryl reagents is prevented by acetyl phosphate in the presence of pyrophosphate or citrate, but not in the presence of arsenate or phosphate.</p></span></li><li><span>4.</span><span><p>4. In the absence of other polyvalent anions, acetyl phosphate alone can stimulate the conversion of NADH into NADH-X at low pH.</p></span></li><li><span>5.</span><span><p>5. In the presence of acetyl phosphate, the relative rate of formation of NAD<sup>+</sup> and NADH-X from NADH is dependent on the pH and the anions present.</p></span></li></ul></div>\",\"PeriodicalId\":100160,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"volume\":\"128 1\",\"pages\":\"Pages 74-81\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1966-10-17\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6593(66)90143-3\",\"citationCount\":\"13\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926659366901433\",\"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 and Biological Oxidation","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926659366901433","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The side activities of d-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating) from rabbit muscle: NADH-X formation
1.
1. The formation of NADH-X from NADH in the presence of glyceraldehyde phosphate dehydrogenase (EC 1.2.1.12) at low pH is observed not only in the presence of pyrophosphate, citrate or phosphate, but also in the presence of arsenate.
2.
2. Stimulation of NADH-X formation by acetyl phosphate is dependent on the presence of enzyme-bound NAD+; however, added NAD+ is inhibitory.
3.
3. Inhibition of NADH-X formation by sulphydryl reagents is prevented by acetyl phosphate in the presence of pyrophosphate or citrate, but not in the presence of arsenate or phosphate.
4.
4. In the absence of other polyvalent anions, acetyl phosphate alone can stimulate the conversion of NADH into NADH-X at low pH.
5.
5. In the presence of acetyl phosphate, the relative rate of formation of NAD+ and NADH-X from NADH is dependent on the pH and the anions present.
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