Production and purification of a recombinant human 14 kDa β-galactoside-binding lectin |
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Authors: | Jun Hirabayashi Hitoshi Ayaki Gen-Ichiro Soma andKen-Ichi Kasai |
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Institution: | Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Kanagawa, Jappan. |
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Abstract: | The cDNA for a 14 kDa human β-galactoside-binding lectin was inserted into a plasmid carrying a taq promoter, and the lectin protein was expressed in E. coli cells. The recombinant lectin was extracted from the cells and purified to apparent homogeneity by a single-step chromatography on an asialofetuin-agarose column. Subunit molecular mass (14 kDa), hemagglutinating activity and antigenicity were indistinguishable from those of the human placental lectin. Though the N-terminal of the placental lectin is blocked with an acetyl group, the recombinant lectin was found to have a free amino group. However, the N-terminal amino acid sequences were identical. The recombinant lectin was considered to have the same three-dimensional structure as the placental lectin. |
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Keywords: | Galactoside binding β- Lectin expression Cell differentiation (Human lung E coli) |
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