• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biotechnology Progress >Use of dye affinity chromatography for the purification of aerococcus viridans lactate oxidase
【24h】

Use of dye affinity chromatography for the purification of aerococcus viridans lactate oxidase

机译：染料亲和色谱法在纯化绿球菌乳酸氧化酶中的应用

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Lactate oxidase was purified from Aerococcus viridans (A.viridans) by dye affinity chromatography and FPLC ion exchange chromatography.The lactate oxidase could be purified by comparatively simple procedures,the purification achieved from a crude extract of A.viridans was 41-fold with a specific activity of 143 units/(mg of protein).The purified enzyme was a L-lactate oxidase,which catalyses the conversion of L-lactate in the presence of moelcular oxygen to pyruvate and H_2O_2.This purified lactate oxidase showed an apparent moelcualr mass of 48 200 in SDS-PAGE and the native molecular weight,as estimated by FPLC gelfiltration,was 187 300.This molecular weight indicates that lactate oxidase exists in tetrameric form after gelfiltration.To differing degrees,all the triazine dyes tested were inhiibtors of lactate oxidase,solutions of free triazine dyes showing aninhibition mechanism which was bot time-and pH-dependent.
机译：通过染料亲和层析和FPLC离子交换层析从绿气球菌中纯化乳酸氧化酶。乳酸氧化酶可以通过相对简单的程序进行纯化，从黄曲霉粗提物中得到的纯化率是41倍。比活度为143单位/（mg蛋白质）。纯化的酶为L-乳酸氧化酶，在存在分子氧的情况下催化L-乳酸转化为丙酮酸和H_2O_2。该纯化的乳酸氧化酶显示出明显的分子质量。 SDS-PAGE中48 200的分子量，通过FPLC凝胶过滤测得的天然分子量为187300。该分子量表明凝胶过滤后，乳酸氧化酶以四聚体形式存在。在不同程度上，所有测试的三嗪染料都是乳酸的抑制剂氧化酶，游离的三嗪染料溶液显示出抑制机制，该机制是由时间和pH决定的。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号