The heparin-binding domain of extracellular superoxide dismutase C and formation of variants with reduced heparin affinity.

@article{Sandstrm1992TheHD,
  title={The heparin-binding domain of extracellular superoxide dismutase C and formation of variants with reduced heparin affinity.},
  author={Jan Sandstr{\"o}m and Lennart Carlsson and Stefan L Marklund and Thomas Edlund},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 25},
  pages={18205-9}
}
A fundamental property of the secretory tetrameric extracellular superoxide dismutase (EC-SOD) is its affinity for heparin and analogues, in vivo, mediating attachment to heparan sulfate proteoglycans located on cell surfaces and in the connective tissue matrix. EC-SOD is in vivo heterogeneous with regard to heparin affinity and can be divided into subclasses; A which lacks heparin affinity, B with intermediate affinity, and C with strong heparin affinity. The EC-SOD C subunits contain 222… CONTINUE READING
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