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Publication Detail
Neutron scattering studies of subcomponent C1q of first component C1 of human complement and its association with subunit C1r2C1s2 within C1
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Perkins SJ, Villiers CL, Arlaud GJ, Boyd J, Burton DR, Colomb MG, Dwek RA
  • Publication date:
  • Pagination:
    547, 557
  • Journal:
    Journal of Molecular Biology
  • Volume:
  • Issue:
  • Status:
  • Print ISSN:
Neutron scattering studies are reported on subcomponent C1q of component C1 of human complement, and on C1, the complex of C1q with subunit C1r2C1s2. For C1q, the molecular weight was determined as 460,000. The radius of gyration at infinite contrast Rc is 12.8 nm. The Rc values for the proteolytically cleaved forms of C1q, namely the heads and the stalks, are 1.5 to 2 nm and 11 nm, respectively, and thus the axis-to-arm angle of C1q is estimated at 45 °. Neutron data for subunit C1r2C1s2 are published elsewhere. The neutron data on C1 lead to an Rc value of 12.6 nm for proenzymic C1 and a molecular weight of 820,000. The wideangle scattering curve of C1q exhibits a minimum at Q = 0.28 nm-1 and a maximum at 0.39 nm-1; on the addition of C1r2C1s2, this minimum disappears. The neutron data on C1 indicate that C1q and C1r2C1s2 have complexed with a large conformational change in one or both parts. No conformational changes can be detected on the activation of C1 by this method. © 1984.
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