来自蚂蚱排泄系统的碱性磷酸酶

Samir M. Khoja
{"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。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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+.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信