Characterisation of the conformational and quaternary structure-dependent heparin-binding region of bovine seminal plasma protein PDC-109.

@article{Calvete1999CharacterisationOT,
  title={Characterisation of the conformational and quaternary structure-dependent heparin-binding region of bovine seminal plasma protein PDC-109.},
  author={Juan J Calvete and Mar{\'i}a Asunci{\'o}n Campanero-Rhodes and Manfred Raida and Laura Sanz},
  journal={FEBS letters},
  year={1999},
  volume={444 2-3},
  pages={
          260-4
        }
}
PDC-109, the major heparin-binding protein of bull seminal plasma, binds to sperm choline lipids at ejaculation and modulates capacitation mediated by heparin. Affinity chromatography on heparin-Sepharose showed that polydisperse, but not monomeric, PDC-109 displayed heparin-binding capability. We sought to characterise the surface topology of the quaternary structure-dependent heparin-binding region of PDC-109 by comparing the arginine- and lysine-selective chemical modification patterns of… CONTINUE READING

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