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Cloning and GST-fused expression in E. coli of mouse beta-1,4-galactosyltransferase.
Gong, Xing-guo; Zhong, Wen-tao; Wu, Wen-ying.
Afiliación
  • Gong XG; Institute of Biomacromolecule & Enzyme Engineering, College of Life Sciences, Zhejiang University, Hangzhou 310027, China. Gongxg@cls.zju.edu.cn
J Zhejiang Univ Sci ; 5(2): 164-72, 2004 Feb.
Article en En | MEDLINE | ID: mdl-14674027
Beta-1,4-galactosyltransferase (beta4Gal-T) (EC 2.4.1.38) plays a multifunctional role in many aspects of normal cell physiology. By now, several dozens of beta4Gal-T genes have been cloned, separated from mouse, chick, bovine, human, etc. This paper presents the cloning and GST-fused expression of mouse beta4Gal-T gene in Escherichia coli (E. coli). The target gene was cloned by PCR, followed by identification by DNA sequencing and expression in E.coli with isopropyl-beta-D-thiogalactoside (IPTG) gradient concentrations, products of which were separated on SDS-PAGE showing that the target protein had the same molecular weight as that of mouse beta4Gal-T. The transcriptional product of beta4Gal-T gene was proved by Western hybridization analysis to be due to GST-fusion.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Clonación Molecular / N-Acetil-Lactosamina Sintasa / Escherichia coli / Glutatión Transferasa Límite: Animals Idioma: En Revista: J Zhejiang Univ Sci Asunto de la revista: CIENCIA Año: 2004 Tipo del documento: Article País de afiliación: China Pais de publicación: China
Buscar en Google
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Clonación Molecular / N-Acetil-Lactosamina Sintasa / Escherichia coli / Glutatión Transferasa Límite: Animals Idioma: En Revista: J Zhejiang Univ Sci Asunto de la revista: CIENCIA Año: 2004 Tipo del documento: Article País de afiliación: China Pais de publicación: China