文章基本信息

标题：Heterologous Expression and Purification of ? Galactosidase Protein Using Affinity Chromatography
其他标题：Heterologous Expression and Purification of ? Galactosidase Protein Using Affinity Chromatography
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作者：M. Z. Alam ; L. Ragionieri ; M. A. S. Santos 等
期刊名称：Journal of Scientific Research
印刷版ISSN：2070-0237
电子版ISSN：2070-0245
出版年度：2013
卷号：5
期号：3
页码：499-513
DOI：10.3329/jsr.v5i3.13820
语种：English
出版社：Rajshahi University
摘要：Enzymes and other protein purification using recombinant DNA technology have become popular due to scarcity of natural protein. Saccharomyces cerevisiae is a demanding host, since it facilitates protein expression by its relative simplicity, safe organisms, inexpensive and has many properties of eukaryotic expression system. As an alternative host we express E. coli lacZ gene with GST tag in Saccharomyces cerevisiae and successfully purified from soluble extracts. The concentration of soluble GST-? galactosidase protein was approximately 0.57 mg/ml of elution buffer yielded from 50 ml yeast cell culture. The ?-galactosidase protein from insoluble extract was low due to the increasing solubility of GST tag. Keywords: ?-galactosidase; Heterologous expression; GST tag; Affinity chromatography. © 2013 JSR Publications. ISSN: 2070-0237 (Print); 2070-0245 (Online). All rights reserved. doi: http://dx.doi.org/10.3329/jsr.v5i3.13820 J. Sci. Res. 5 (3), 499-513 (2013)
关键词：Biology; Genetic Engineering and Biotechnology;?-galactosidase; Heterologous expression; GST tag; Affinity chromatography.