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Conformational change of complement proteins C3 and C4 induced by methylamine: An X-ray scattering study

Österberg, R. ; Eggertsen, G. ; Lundwall, Åke LU and Sjöquist, J. (1984) In International Journal of Biological Macromolecules 6. p.8-195
Abstract
Analysis of X-ray scattering data from dilute solutions of the complement proteins C3, C4 and C5 yields the radii of gyration 4.5, 4.25 and 4.8 nm, and the maximum distances within the molecules (Dmax) of 18, 14.5 and 14 nm, respectively. The X-ray data of C4 are compatible with the scattering from one single triaxial body represented as an elliptic cylinder with the semiaxes 5.6 and 2.1 nm and a length of 11.0 nm. When C3 and c4 react with methylamine, at pH 8.0, the radii of gyration increase to 5.1 and 4.2 nm, and the Dmax)-values increase to 25 and 18 nm, respectively; for C5 there was no noticeable change in the X-ray scattering curve. The methylamine reactions are discussed in relation to conformational changes and possible... (More)
Analysis of X-ray scattering data from dilute solutions of the complement proteins C3, C4 and C5 yields the radii of gyration 4.5, 4.25 and 4.8 nm, and the maximum distances within the molecules (Dmax) of 18, 14.5 and 14 nm, respectively. The X-ray data of C4 are compatible with the scattering from one single triaxial body represented as an elliptic cylinder with the semiaxes 5.6 and 2.1 nm and a length of 11.0 nm. When C3 and c4 react with methylamine, at pH 8.0, the radii of gyration increase to 5.1 and 4.2 nm, and the Dmax)-values increase to 25 and 18 nm, respectively; for C5 there was no noticeable change in the X-ray scattering curve. The methylamine reactions are discussed in relation to conformational changes and possible dimerizations of C3 and C4. (Less)
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publishing date
type
Contribution to journal
publication status
published
subject
in
International Journal of Biological Macromolecules
volume
6
pages
8 - 195
publisher
Elsevier
external identifiers
  • scopus:0021207870
ISSN
1879-0003
language
English
LU publication?
no
id
8fd6f36c-a061-4962-b59f-813a7de2d3d9 (old id 3965069)
date added to LUP
2016-04-04 13:34:17
date last changed
2021-01-03 09:54:19
@article{8fd6f36c-a061-4962-b59f-813a7de2d3d9,
  abstract     = {{Analysis of X-ray scattering data from dilute solutions of the complement proteins C3, C4 and C5 yields the radii of gyration 4.5, 4.25 and 4.8 nm, and the maximum distances within the molecules (Dmax) of 18, 14.5 and 14 nm, respectively. The X-ray data of C4 are compatible with the scattering from one single triaxial body represented as an elliptic cylinder with the semiaxes 5.6 and 2.1 nm and a length of 11.0 nm. When C3 and c4 react with methylamine, at pH 8.0, the radii of gyration increase to 5.1 and 4.2 nm, and the Dmax)-values increase to 25 and 18 nm, respectively; for C5 there was no noticeable change in the X-ray scattering curve. The methylamine reactions are discussed in relation to conformational changes and possible dimerizations of C3 and C4.}},
  author       = {{Österberg, R. and Eggertsen, G. and Lundwall, Åke and Sjöquist, J.}},
  issn         = {{1879-0003}},
  language     = {{eng}},
  pages        = {{8--195}},
  publisher    = {{Elsevier}},
  series       = {{International Journal of Biological Macromolecules}},
  title        = {{Conformational change of complement proteins C3 and C4 induced by methylamine: An X-ray scattering study}},
  volume       = {{6}},
  year         = {{1984}},
}