Purification of the growth hormone releasing hormone receptor with a C-terminal, biotinylated affinity ligand.

@article{Zysk1996PurificationOT,
  title={Purification of the growth hormone releasing hormone receptor with a C-terminal, biotinylated affinity ligand.},
  author={John R. Zysk and Bruce D Gaylinn and Charles E. Lyons and Bennett Johnson and C. Mark Eppler and William R Baumbach and Michael O. Thorner},
  journal={Biochemical and biophysical research communications},
  year={1996},
  volume={221 1},
  pages={133-9}
}
The receptor for growth hormone-releasing hormone (GHRH) has been purified from bovine pituitary tissue and HEK293 cells transfected with human or porcine receptor using a retrievable biotinylated GHRH analog. Custom synthesized [His1, Nle27, Biotin-Lys41]-human GHRH-(1-41)-NH2 (GHRHb) bound to pituitary membranes with affinity comparable to human GHRH. GHRHb which has the biotinyl group on the C-terminus of the peptide allowed simultaneous binding to both the receptor and streptavidin agarose… CONTINUE READING

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