Purification and processing of cellulose-binding domain-alkaline phosphatase fusion proteins.

@article{Greenwood1994PurificationAP,
  title={Purification and processing of cellulose-binding domain-alkaline phosphatase fusion proteins.},
  author={Jaclyn M Greenwood and Neil R. Gilkes and Robert C. Miller and Douglas G. Kilburn and Richard A. Warren},
  journal={Biotechnology and bioengineering},
  year={1994},
  volume={44 11},
  pages={1295-305}
}
Fusion of the leader peptide and the cellulose-binding domain (CBD) of endoglucanase A (CenA) from Cellulomonas fimi, with of without linker sequences, to the N-terminus of alkaline phosphatase (PhoA) from Escherichia coli leads to the accumulation of significant amounts of the CBD-PhoA fusion proteins in the supernatants of E. coli cultures. The fusion proteins can be purified from the supernatants by affinity chromatography on cellulose. The fusion protein can be desorbed from the cellulose… CONTINUE READING