会议专题

糖基化酶的糖基改性及其催化多样性的研究

  Contrastive analysis of the β-glucuronidases expressed by different expression systems-three original strains, the prokaryotic and eukaryotic expression system of Pgus showed some differences among the molecular weights, enzymatic properties and models of catalytic reactions these enzymes. It can be speculated that the proteins were glycosylation modified in certain degree and in different ways after produced.The modification changed the protein structure and further the identification between the enzyme and the substrate molecule. As a result, it changed the models of catalytic reactions and the enzymatic properties of the β-glucuronidases.

糖基化酶 糖基改性 催化多样性

LI Chun 李春

School of Life Science and Technology,Beijing Institute of Technology,Beijing 100081 北京理工大学生命科学与技术学院生物工程系

国内会议

第五届全国化学工程与生物化工年会

西安

中文

195-196

2008-10-01(万方平台首次上网日期,不代表论文的发表时间)