Expression and characterization of cysteine-modified variants of an amino-terminal fragment of bactericidal/permeability-increasing protein.

@article{Horwitz1996ExpressionAC,
  title={Expression and characterization of cysteine-modified variants of an amino-terminal fragment of bactericidal/permeability-increasing protein.},
  author={Arnold H. Horwitz and Stefan D. Leigh and S L Abrahamson and HELENE GAZZANO-SANTORO and Pei Shu Liu and Robert E. Williams and Stephen F. Carroll and Georgia Theofan},
  journal={Protein expression and purification},
  year={1996},
  volume={8 1},
  pages={28-40}
}
rBPI23 is a biologically active, recombinant N-terminal fragment of human bactericidal/permeability-increasing protein (BPI). While rBPI23 is readily purified from culture supernatants of Chinese hamster ovary (CHO)-K1 transfectants, it is heterogeneous, consisting of monomer and disulfide-linked dimer, characteristics due presumably to the presence of three cysteines within the molecule. We have examined the role of these cysteines in rBPI23 expression, function, and dimer formation by… CONTINUE READING

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