Research article summary (published 18 Oct 2009):

Thermodynamic characterization of the interaction between the C-terminal domain of extracellular superoxide dismutase and heparin by isothermal titration calorimetry.

Full Abstract

Extracellular superoxide dismutase (ECSOD) interacts with heparin through its C-terminal domain. In this study we used isothermal titration calorimetry (ITC) to get detailed thermodynamic information about the interaction. We have shown that the interaction between ECSOD and intestinal mucosal heparin (M(w) 6000-30000 Da) is exothermic and driven by enthalpy at physiological salt concentration. However, the contribution from entropy is favorable for binding of small isolated heparin fragments. By studying different size-defined heparin fragments, we also concluded that a hexasaccharide moiety is sufficient for strong binding to ECSOD. The binding involves proton transfer from the buffer to the ECSOD-heparin complex, and the results indicate that the number of ionic interactions made between ECSOD and heparin upon binding varies from three to five for heparin and an octasaccharide fragment, respectively. Surprisingly and despite the many charges found on both the protein and the polysaccharide, our results indicate that the nonionic contribution to the binding is large. From the temperature dependence we have calculated the constant pressure heat capacity change (DeltaC(p)) of the interaction to -644 J K(-1) mol(-1) and -306 J K(-1) mol(-1) for heparin and an octasaccharide, respectively.

Author information

Author/s: Ahl, Ing-Marie (IM); Jonsson, Bengt-Harald (BH); Tibell, Lena A E (LA);

Affiliation: Department of Clinical and Experimental Medicine, Linköping University, Sweden.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Biochemistry (Biochemistry), published in United States. (Language: eng)

Reference: 2009-Oct; vol 48 (issue 41) : pp 9932-40

Dates: Created 2009/10/13; Completed 2009/11/02;

PMID: 19754153, status: MEDLINE (last retrieval date: 11/2/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Amino Acid Sequence Animals Binding Sites Buffers Calorimetry - methods Heparin - chemistry; isolation & purification; metabolism Humans Intestinal Mucosa - chemistry

Intestinal Mucosa - chemistry Kinetics Molecular Sequence Data Peptide Fragments - chemistry; metabolism Sodium Chloride - pharmacology Superoxide Dismutase - chemistry; metabolism Swine Thermodynamics

Associated Chemicals: Buffers (0) ; Peptide Fragments (0) ; Sodium Chloride (7647-14-5) ; Heparin (9005-49-6) ; SOD3 protein, human (EC 1.15.1.1) ; Superoxide Dismutase (EC 1.15.1.1)

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