Expression of human milk beta-casein in Escherichia coli: comparison of recombinant protein with native isoforms.

@article{Hansson1993ExpressionOH,
  title={Expression of human milk beta-casein in Escherichia coli: comparison of recombinant protein with native isoforms.},
  author={Lars Ingvar Hansson and Sven Bergstr{\"o}m and Olle Hernell and B O L{\"o}nnerdal and Anna Karin Nilsson and Mats Str{\"o}mqvist},
  journal={Protein expression and purification},
  year={1993},
  volume={4 5},
  pages={373-81}
}
Studies on physiological function and on structure-function relationships of human milk beta-casein have been limited. In this study, we have introduced the human beta-casein cDNA into vectors designed for expression in Escherichia coli. The inducible T7-based expression system resulted in high-level expression of recombinant beta-casein. The recombinant beta-casein, localized intracellularly in E. coli, was purified to homogeneity and compared with purified native beta-casein, in particular… CONTINUE READING

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