Recombinant HMG1 protein produced in Pichia pastoris: a nonviral gene delivery agent.

@article{Mistry1997RecombinantHP,
  title={Recombinant HMG1 protein produced in Pichia pastoris: a nonviral gene delivery agent.},
  author={Anita R Mistry and Luigi Falciola and Luc{\'i}a Monaco and R Tagliabue and Giulia Acerbis and Andrew Knight and Richard Paul Harbottle and Marco S{\'o}ria and Marco Emilio Bianchi and Charles Coutelle and Stephen L Hart},
  journal={BioTechniques},
  year={1997},
  volume={22 4},
  pages={
          718-29
        }
}
This paper describes the production of a recombinant protein from the expression system based on the methylotrophic yeast Pichia pastoris. Efficient production of rat high-mobility-group 1 (HMG1) protein was obtained using the system. Two forms of HMG1 were secreted into the culture medium: a 24.5-kDa species corresponding to the native HMG1 and a 32-kDa glycosylated derivative. Non-glycosylated recombinant HMG1 was purified easily and shown to possess the same DNA-binding properties as HMG1… CONTINUE READING

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