{"title":"羟基离子对大鼠肝微粒体葡萄糖6-磷酸酶、无机焦磷酸酶和无机焦磷酸酶-葡萄糖磷酸转移酶的激活作用","authors":"Marjorie R. Stetten, Foster F. Burnett","doi":"10.1016/0926-6593(66)90181-0","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. OH- has been shown to produce a 2- to 3-fold increase in the apparent activity <em>in vitro</em> of rat-liver microsomal glucose 6-phosphatase (EC 3.1.3.9) and the related enzymatic activities, inorganic pyrophosphatase, inorganic pyrophosphate-glucose phosphotransferase and adenosine-5′-triphosphate-glucose phosphotransferase.</p></span></li><li><span>2.</span><span><p>2. Optimal activation is achieved by pre-treatment of liver microsomes with ammonium or amino acid buffers at pH 9.5–9.8. Inactivation is observed above pH 10.</p></span></li><li><span>3.</span><span><p>3. This activation is as great or greater than that produced by deoxycholate or Triton X-100 treatment and the thermal instability introduced by these reagents is avoided.</p></span></li><li><span>4.</span><span><p>4. Alteration of the microsomal membranes by treatment with base is accompanied by a decrease in turbidity but does not result in a solubilization of the enzyme. The essential protein-lipid binding is apparently retained and the enzyme, so treated, is relatively stable at 30°.</p></span></li><li><span>5.</span><span><p>5. NH<sub>4</sub>OH pretreatment of microsomes results in a lowering of the apparent Michaelis constant for glucose 6-phosphatase, similar to that caused by digitonin, deoxycholate and Triton X-100.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 2","pages":"Pages 344-350"},"PeriodicalIF":0.0000,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90181-0","citationCount":"51","resultStr":"{\"title\":\"Activation of rat-liver microsomal glucose 6-phosphatase, inorganic pyrophosphatase and inorganic pyrophosphate-glucose phosphotransferase by hydroxyl ion\",\"authors\":\"Marjorie R. Stetten, Foster F. Burnett\",\"doi\":\"10.1016/0926-6593(66)90181-0\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. OH- has been shown to produce a 2- to 3-fold increase in the apparent activity <em>in vitro</em> of rat-liver microsomal glucose 6-phosphatase (EC 3.1.3.9) and the related enzymatic activities, inorganic pyrophosphatase, inorganic pyrophosphate-glucose phosphotransferase and adenosine-5′-triphosphate-glucose phosphotransferase.</p></span></li><li><span>2.</span><span><p>2. Optimal activation is achieved by pre-treatment of liver microsomes with ammonium or amino acid buffers at pH 9.5–9.8. Inactivation is observed above pH 10.</p></span></li><li><span>3.</span><span><p>3. This activation is as great or greater than that produced by deoxycholate or Triton X-100 treatment and the thermal instability introduced by these reagents is avoided.</p></span></li><li><span>4.</span><span><p>4. Alteration of the microsomal membranes by treatment with base is accompanied by a decrease in turbidity but does not result in a solubilization of the enzyme. The essential protein-lipid binding is apparently retained and the enzyme, so treated, is relatively stable at 30°.</p></span></li><li><span>5.</span><span><p>5. NH<sub>4</sub>OH pretreatment of microsomes results in a lowering of the apparent Michaelis constant for glucose 6-phosphatase, similar to that caused by digitonin, deoxycholate and Triton X-100.</p></span></li></ul></div>\",\"PeriodicalId\":100160,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"volume\":\"128 2\",\"pages\":\"Pages 344-350\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1966-11-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6593(66)90181-0\",\"citationCount\":\"51\",\"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/0926659366901810\",\"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/0926659366901810","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Activation of rat-liver microsomal glucose 6-phosphatase, inorganic pyrophosphatase and inorganic pyrophosphate-glucose phosphotransferase by hydroxyl ion
1.
1. OH- has been shown to produce a 2- to 3-fold increase in the apparent activity in vitro of rat-liver microsomal glucose 6-phosphatase (EC 3.1.3.9) and the related enzymatic activities, inorganic pyrophosphatase, inorganic pyrophosphate-glucose phosphotransferase and adenosine-5′-triphosphate-glucose phosphotransferase.
2.
2. Optimal activation is achieved by pre-treatment of liver microsomes with ammonium or amino acid buffers at pH 9.5–9.8. Inactivation is observed above pH 10.
3.
3. This activation is as great or greater than that produced by deoxycholate or Triton X-100 treatment and the thermal instability introduced by these reagents is avoided.
4.
4. Alteration of the microsomal membranes by treatment with base is accompanied by a decrease in turbidity but does not result in a solubilization of the enzyme. The essential protein-lipid binding is apparently retained and the enzyme, so treated, is relatively stable at 30°.
5.
5. NH4OH pretreatment of microsomes results in a lowering of the apparent Michaelis constant for glucose 6-phosphatase, similar to that caused by digitonin, deoxycholate and Triton X-100.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
