{"title":"来自蚂蚱排泄系统的碱性磷酸酶","authors":"Samir M. Khoja","doi":"10.1016/0020-1790(91)90012-4","DOIUrl":null,"url":null,"abstract":"<div><p>Alkaline phosphatase from the excretory system of the grasshopper, <em>Poekilocerus bufonius</em> was purified with ammonium sulphate fractionation and chromatography on Bio-Gel A-0.5 m. The specific activity of the enzyme is 152 units/mg of protein. The enzyme is a tetramer and the <em>M</em><sub>r</sub> value of the subunit is 72,000 ± 2500 as shown by gel filtration and SDS-polyacrylamide gel electrophoresis. The enzyme has a pH optimum of 9.6 and an apparent <em>K</em><sub>m</sub> value of 0.28 × 10<sup>−3</sup> M. The activity of the enzyme reached a maximum at 75°C and the enzyme showed stability at 65°C. The enzyme was inhibited by Ca<sup>2+</sup>, Na<sup>+</sup> and Fe<sup>3+</sup> and was stimulated by Zn<sup>2+</sup>, Mn<sup>2+</sup> and Mg<sup>2+</sup>.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 3","pages":"Pages 239-242"},"PeriodicalIF":0.0000,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90012-4","citationCount":"8","resultStr":"{\"title\":\"Alkaline phosphatase from the excretory system of the grasshopper, Poekilocerus bufonius\",\"authors\":\"Samir M. Khoja\",\"doi\":\"10.1016/0020-1790(91)90012-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Alkaline phosphatase from the excretory system of the grasshopper, <em>Poekilocerus bufonius</em> was purified with ammonium sulphate fractionation and chromatography on Bio-Gel A-0.5 m. The specific activity of the enzyme is 152 units/mg of protein. The enzyme is a tetramer and the <em>M</em><sub>r</sub> value of the subunit is 72,000 ± 2500 as shown by gel filtration and SDS-polyacrylamide gel electrophoresis. The enzyme has a pH optimum of 9.6 and an apparent <em>K</em><sub>m</sub> value of 0.28 × 10<sup>−3</sup> M. The activity of the enzyme reached a maximum at 75°C and the enzyme showed stability at 65°C. The enzyme was inhibited by Ca<sup>2+</sup>, Na<sup>+</sup> and Fe<sup>3+</sup> and was stimulated by Zn<sup>2+</sup>, Mn<sup>2+</sup> and Mg<sup>2+</sup>.</p></div>\",\"PeriodicalId\":13955,\"journal\":{\"name\":\"Insect Biochemistry\",\"volume\":\"21 3\",\"pages\":\"Pages 239-242\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0020-1790(91)90012-4\",\"citationCount\":\"8\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Insect Biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0020179091900124\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Insect Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0020179091900124","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 8
摘要
从蚱蜢排泄系统中提取碱性磷酸酶,采用硫酸铵分离和A-0.5 m Bio-Gel层析纯化。该酶的比活性为152单位/毫克蛋白质。该酶为四聚体,经凝胶过滤和sds -聚丙烯酰胺凝胶电泳,其亚基Mr值为72000±2500。酶的最适pH值为9.6,表观Km值为0.28 × 10−3 m,酶的活性在75℃时达到最大值,在65℃时表现出稳定性。该酶受Ca2+、Na+和Fe3+的抑制,受Zn2+、Mn2+和Mg2+的刺激。
Alkaline phosphatase from the excretory system of the grasshopper, Poekilocerus bufonius
Alkaline phosphatase from the excretory system of the grasshopper, Poekilocerus bufonius was purified with ammonium sulphate fractionation and chromatography on Bio-Gel A-0.5 m. The specific activity of the enzyme is 152 units/mg of protein. The enzyme is a tetramer and the Mr value of the subunit is 72,000 ± 2500 as shown by gel filtration and SDS-polyacrylamide gel electrophoresis. The enzyme has a pH optimum of 9.6 and an apparent Km value of 0.28 × 10−3 M. The activity of the enzyme reached a maximum at 75°C and the enzyme showed stability at 65°C. The enzyme was inhibited by Ca2+, Na+ and Fe3+ and was stimulated by Zn2+, Mn2+ and Mg2+.