Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12452443
DOI
10.1515/bc.2002.187
Knihovny.cz E-resources
- MeSH
- Protein Denaturation MeSH
- Haptoglobins chemistry metabolism MeSH
- Hemoglobins chemistry MeSH
- Catalase chemistry MeSH
- Humans MeSH
- Molecular Chaperones chemistry metabolism MeSH
- Models, Molecular MeSH
- Molecular Sequence Data MeSH
- Heat-Shock Proteins chemistry metabolism MeSH
- Solvents chemistry MeSH
- Protein Structure, Secondary MeSH
- Amino Acid Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Sequence Alignment MeSH
- Spectrum Analysis MeSH
- Thermodynamics MeSH
- Titrimetry MeSH
- Binding Sites MeSH
- Hot Temperature MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Haptoglobins MeSH
- Hemoglobins MeSH
- Catalase MeSH
- Molecular Chaperones MeSH
- Heat-Shock Proteins MeSH
- Solvents MeSH
With respect to the mechanism of chaperone-like activity, we examined the behavior of haptoglobin under heat shock conditions. Secondary structure changes during heat treatment were followed by circular dichroism, Raman and infrared spectroscopy. A model of the haptoglobin tetramer, based on its sequence homology with serine proteases and the CCP modules, has been proposed. Sequence regions responsible for the chaperone-like activity were not fully identical with the region that takes part in formation of the hemoglobin-haptoglobin complex. We can postulate the presence of at least two different chaperone-binding sites on each haptoglobin heavy chain.
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