Efficient production of recombinant human pleiotrophin in yeast, Pichia pastoris
A Murasugi, I Kido, H Kumai, Y Asami - Bioscience, biotechnology …, 2003 - jstage.jst.go.jp
A Murasugi, I Kido, H Kumai, Y Asami
Bioscience, biotechnology, and biochemistry, 2003•jstage.jst.go.jpApproximately 260 mgWl of authentic recombinant human pleiotrophin (rhPTN) was
expressed into the medium of highcell density fermentation using a Pichia pastoris protein
expression system. The prepro sequence of yeast amating factor was used successfully. The
recombinant hPTN was e ciently recovered from the medium by expanded bed adsorption,
and puri ed using successive column chromatography steps. In the puri ed rhPTN
preparation, modi ed rhPTN were scarcely detected. Circular dichroism measurement of the …
expressed into the medium of highcell density fermentation using a Pichia pastoris protein
expression system. The prepro sequence of yeast amating factor was used successfully. The
recombinant hPTN was e ciently recovered from the medium by expanded bed adsorption,
and puri ed using successive column chromatography steps. In the puri ed rhPTN
preparation, modi ed rhPTN were scarcely detected. Circular dichroism measurement of the …
Approximately 260 mgWl of authentic recombinant human pleiotrophin (rhPTN) was expressed into the medium of highcell density fermentation using a Pichia pastoris protein expression system. The prepro sequence of yeast amating factor was used successfully. The recombinant hPTN was e ciently recovered from the medium by expanded bed adsorption, and puri ed using successive column chromatography steps. In the puri ed rhPTN preparation, modi ed rhPTN were scarcely detected. Circular dichroism measurement of the puri ed PTN showed the presence of the character istic bstructures in the protein.
jstage.jst.go.jp