Purification and functional characterization of integrin alpha v beta 5. An adhesion receptor for vitronectin.

@article{Smith1990PurificationAF,
  title={Purification and functional characterization of integrin alpha v beta 5. An adhesion receptor for vitronectin.},
  author={Jeffrey W. Smith and Deborah J. Vestal and Sandra Irwin and Timothy A Burke and David A. Cheresh},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 19},
  pages={11008-13}
}
We have purified a novel member of the integrin gene family from placenta that serves as a vitronectin receptor. This integrin is composed of the alpha v subunit and a beta subunit that we designate beta 5. Purification was accomplished by immunodepleting a placental extract of integrin alpha v beta 3, allowing us to purify alpha v beta 5 from the remaining extract by monoclonal antibody affinity chromatography on LM 142-Sepharose, which binds to the alpha v subunit. Purification to homogeneity… CONTINUE READING

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