Isolation and characterization of ovine IGFBP-4: protein purification and cDNA sequence.

@article{Carr1994IsolationAC,
  title={Isolation and characterization of ovine IGFBP-4: protein purification and cDNA sequence.},
  author={Jessica M Carr and Patricia A Grant and Geoffrey Leonard Francis and Julie A Owens and J. C. Wallace and P W Walton},
  journal={Journal of molecular endocrinology},
  year={1994},
  volume={13 2},
  pages={219-36}
}
Three different molecular mass forms of IGF-binding proteins (IGFBPs) were purified from ovine plasma by IGF-I affinity chromatography and reverse-phase HPLC: a 46 kDa doublet and 29 kDa and 24 kDa forms. Amino-terminal sequence analysis confirmed that these proteins were ovine (o)IGFBP-3 (46 kDa) and two molecular size variants of oIGFBP-4. oIGFBP-3 and the 29 kDa form of oIGFBP-4 were shown to be N-glycosylated. Isoelectric points were determined to be at approximately pH 6 for oIGFBP-3 and… CONTINUE READING

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