Characterization of high affinity progesterone-binding membrane proteins by an anti-peptide antiserum

@article{Meyer1998CharacterizationOH,
  title={Characterization of high affinity progesterone-binding membrane proteins by an anti-peptide antiserum},
  author={C. Meyer and R. Schmid and K. Schmieding and E. Falkenstein and M. Wehling},
  journal={Steroids},
  year={1998},
  volume={63},
  pages={111-116}
}
  • C. Meyer, R. Schmid, +2 authors M. Wehling
  • Published 1998
  • Biology, Medicine
  • Steroids
  • A chemically synthesized 15-mer oligopeptide derived from the N terminus of high affinity progesterone-binding membrane site(s) from porcine liver was used to generate site-specific antibodies. Western blotting experiments confirmed the specificity of the anti-peptide serum obtained. In further investigations this antiserum was used for the identification of the native progesterone-binding membrane protein complex that represents an oligomer with an apparent molecular mass of about 200 kDa. In… CONTINUE READING
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