Purification and biochemical characterization of recombinant alpha 1-antitrypsin variants expressed in Escherichia coli.

@article{Bischoff1991PurificationAB,
  title={Purification and biochemical characterization of recombinant alpha 1-antitrypsin variants expressed in Escherichia coli.},
  author={Rainer Bischoff and Dexter Speck and Pierre Lepage and L Delatre and Corinne Ledoux and Spencer W. Brown and C A Roitsch},
  journal={Biochemistry},
  year={1991},
  volume={30 14},
  pages={3464-72}
}
Site-directed variants of alpha 1-antitrypsin (alpha 1AT) expressed in a recombinant strain of Escherichia coli have been isolated with an overall process yield of 50% following tangential flow ultrafiltration, anion-exchange, immobilized metal affinity, and hydrophobic interaction chromatography. The primary structure of the purified variants including the integrity of the N- and C-termini has been verified by electrospray mass spectrometry of the intact molecules (44 kDa) for two of the… CONTINUE READING