• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

用活性磁性修饰剂对酶进行化学修饰。

Chemical modification of enzymes with activated magnetic modifier.

作者信息

Yoshimoto T, Mihama T, Takahashi K, Saito Y, Tamaura Y, Inada Y

出版信息

Biochem Biophys Res Commun. 1987 Jun 15;145(2):908-14. doi: 10.1016/0006-291x(87)91051-5.

DOI:10.1016/0006-291x(87)91051-5
PMID:3593378
Abstract

An activated magnetic modifier, which could render biological materials magnetic property, was synthesized in following two steps: oxidation of ferrous ions (Fe2+) with hydrogen peroxide in the presence of alpha, omega-dicarboxymethylpoly(oxyethylene) (DCPEG) to obtain DCPEG-magnetite (Fe3O4); free carboxyl groups in the DCPEG-magnetite were activated with N-hydroxysuccinimide. By coupling the activated magnetic modifier to amino groups of lipase or L-asparaginase, magnetic enzymes were prepared. They dispersed stably not only in aqueous solution but also in organic solvents with high enzymic activities. Magnetic enzymes were readily recovered from reaction mixture in a magnetic field of 6000 Oe without loss of enzymic activity.

摘要

一种能够赋予生物材料磁性的活性磁性修饰剂,通过以下两步合成:在α,ω-二羧甲基聚(氧乙烯)(DCPEG)存在下,用过氧化氢氧化亚铁离子(Fe2+)以获得DCPEG-磁铁矿(Fe3O4);用N-羟基琥珀酰亚胺活化DCPEG-磁铁矿中的游离羧基。通过将活性磁性修饰剂与脂肪酶或L-天冬酰胺酶的氨基偶联,制备了磁性酶。它们不仅能稳定地分散在水溶液中,还能分散在具有高酶活性的有机溶剂中。在6000奥斯特的磁场中,磁性酶很容易从反应混合物中回收,且酶活性不会丧失。

相似文献

1
Chemical modification of enzymes with activated magnetic modifier.用活性磁性修饰剂对酶进行化学修饰。
Biochem Biophys Res Commun. 1987 Jun 15;145(2):908-14. doi: 10.1016/0006-291x(87)91051-5.
2
Magnetic lipase active in organic solvents.在有机溶剂中具有活性的磁性脂肪酶。
Biochem Biophys Res Commun. 1987 Jan 30;142(2):291-6. doi: 10.1016/0006-291x(87)90271-3.
3
Fibrinolysis by urokinase endowed with magnetic property.具有磁性的尿激酶介导的纤维蛋白溶解作用。
Biochem Biophys Res Commun. 1987 Oct 14;148(1):392-6. doi: 10.1016/0006-291x(87)91123-5.
4
[Effect of several factors on enzymic activity and antigenicity in chemical modification of L-asparaginase].[几种因素对L-天冬酰胺酶化学修饰中酶活性及抗原性的影响]
Yao Xue Xue Bao. 1990;25(10):732-8.
5
[PEGylated recombinant L-asparaginase from Erwinia carotovora: Production, properties, and potential applications].[来自胡萝卜软腐欧文氏菌的聚乙二醇化重组L-天冬酰胺酶:生产、性质及潜在应用]
Prikl Biokhim Mikrobiol. 2017 Mar-Apr;53(2):164-72.
6
[PEG-chitosan branched copolymers to improve the biocatalytic properties of Erwinia carotovora recombinant L-asparaginase].[聚乙二醇-壳聚糖支链共聚物用于改善胡萝卜软腐欧文氏菌重组L-天冬酰胺酶的生物催化特性]
Biomed Khim. 2015 Jul-Aug;61(4):480-7. doi: 10.18097/PBMC20156104480.
7
In situ preparation of magnetic Fe3O4-chitosan nanoparticles for lipase immobilization by cross-linking and oxidation in aqueous solution.通过在水溶液中交联和氧化原位制备用于固定化脂肪酶的磁性Fe3O4-壳聚糖纳米颗粒。
Bioresour Technol. 2009 Jul;100(14):3459-64. doi: 10.1016/j.biortech.2009.02.018. Epub 2009 Mar 28.
8
Modification of proteins with polyethylene glycol derivatives.用聚乙二醇衍生物对蛋白质进行修饰。
Methods Enzymol. 1994;242:65-90. doi: 10.1016/0076-6879(94)42009-2.
9
[Preparation of repeatedly and effectively usable L-asparaginase by a chemical modification].[通过化学修饰制备可重复有效使用的L-天冬酰胺酶]
Gan To Kagaku Ryoho. 1984 Oct;11(10):2227-35.
10
Chemical modification of L-asparaginase with a comb-shaped copolymer of polyethylene glycol derivative and maleic anhydride.用聚乙二醇衍生物与马来酸酐的梳状共聚物对L-天冬酰胺酶进行化学修饰。
Biochem Biophys Res Commun. 1992 Apr 15;184(1):144-8. doi: 10.1016/0006-291x(92)91170-u.

引用本文的文献

1
Development of systems for targeting the regional lymph nodes for diagnostic imaging: in vivo behaviour of colloidal PEG-coated magnetite nanospheres in the rat following interstitial administration.
Pharm Res. 2001 May;18(5):640-5. doi: 10.1023/a:1011081210142.
2
Immobilization of protein on ferromagnetic Dacron.蛋白质在铁磁性涤纶上的固定化。
Appl Biochem Biotechnol. 1991 Oct;31(1):53-8. doi: 10.1007/BF02922125.