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Characterization of the Heparin Binding of Human Extracellular Superoxide Dismutase
Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Division of cell biology.ORCID iD: 0000-0002-4694-5611
Medical chemistry Umeå.
Biochemistry Umeå.
2000 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 39, 230-236 p.Article in journal (Refereed) Published
Abstract [en]

 The C-terminal domain of human extracellular superoxide dismutase (hEC-SOD) plays a crucial role in the protein's interaction with heparin. Here we investigated this interaction in more detail by comparing the heparin-binding characteristics of two variants of hEC-SOD: the two fusion proteins containing the hEC-SOD C-terminal domain and a synthetic peptide homologous to the C-terminal. The interaction studies were performed using a surface plasmon resonance based technique on a BIAcore system. It should be emphasized that this is a model system. However, the kinetic constants, as measured, are valid in a comparative sense. Comparison of affinities for size-fractionated heparins revealed that octa- or decasaccharides are the smallest heparin fragments that can efficiently interact with the C-terminal domain of hEC-SOD. At physiological salt concentration, and pH 7.4, the hEC-SOD/heparin interaction was found to be of a high-affinity type, with an equilibrium dissociation constant, Kd, of 0.12 M, which is 700 and 10-20 times lower than the Kd values for the synthetic peptide and the fusion proteins, respectively. However, when an -helical structure was induced in the synthetic peptide, by addition of 10% trifluoroethanol, the Kd decreased to 0.64 M. The differences in the Kd values were mainly governed by differences in the association rate constants (kass). The hEC-SOD/heparin interaction itself was found to have a fairly high dissociation rate constant (0.1 s-1), and a very high association rate constant (8 × 105 M-1 s-1), suggesting that the interaction is mainly controlled by the association. These results together with circular dichroism spectra of the synthetic peptide suggest that an -helical structure in the C-terminal is essential for optimal binding to heparin and that other parts of hEC-SOD moderate the affinity. Our data also demonstrate that the tetramerization itself does not substantially increase the affinity.

Place, publisher, year, edition, pages
2000. Vol. 39, 230-236 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-39492Local ID: 49032OAI: oai:DiVA.org:liu-39492DiVA: diva2:260341
Available from: 2009-10-10 Created: 2009-10-10 Last updated: 2017-12-13

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Tibell, Lena

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