Nygren Babol, Linnea
- Department of Molecular Sciences, Swedish University of Agricultural Sciences
Research article2011Peer reviewed
Holm, Jan; Schou, Christian; Nygren Babol, Linnea; Lawaetz, Anders J.; Bruun, Susanne W.; Hansen, Morten Z.; Hansen, Steen I.
General significance: Self-association into multimers may protect binding sites, and in case of holo-FBP even folate from biological degradation. High-affinity folate binding in body secretions, typically containing 1-10 nM FBP, requires the presence of natural detergents, i.e. cholesterol and phospholipids, to avoid complexation between apo- and holo-FBP. (C) 2011 Elsevier B.V. All rights reserved.
Folate binding protein; Ligand mediated self-association; Asymmetric apo-holo complexes; Surface plasmon resonance; Detergent-tryptophan interaction; Fluorescence spectroscopy
Biochimica et biophysica acta G. General subjects
2011, Volume: 1810, number: 12, pages: 1330-1339
Publisher: ELSEVIER SCIENCE BV
Biochemistry and Molecular Biology
Biophysics
DOI: https://doi.org/10.1016/j.bbagen.2011.07.005
https://res.slu.se/id/publ/46025