Homodimerization of soluble guanylyl cyclase subunits. Dimerization analysis using a glutathione s-transferase affinity tag.

@article{Zabel1999HomodimerizationOS,
  title={Homodimerization of soluble guanylyl cyclase subunits. Dimerization analysis using a glutathione s-transferase affinity tag.},
  author={Ulrike Zabel and Christa Haeusler and Marie-Dominique Weeger and Harald H. H. W. Schmidt},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 26},
  pages={18149-52}
}
Soluble guanylyl cyclase (sGC) is an alpha/beta-heterodimeric hemoprotein that, upon interaction with the intercellular messenger molecule NO, generates cGMP. Although the related family of particulate guanylyl cyclases (pGCs) forms active homodimeric complexes, it is not known whether homodimerization of sGC subunits occurs. We report here the expression in Sf9 cells of glutathione S-transferase-tagged recombinant human sGCalpha1 and beta1 subunits, applying a novel and rapid purification… CONTINUE READING
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