Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Catalase / chemistry
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Haptoglobins / chemistry*
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Haptoglobins / metabolism
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Heat-Shock Proteins / chemistry*
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Heat-Shock Proteins / metabolism
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Hemoglobins / chemistry
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Hot Temperature
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Humans
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Models, Molecular
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Molecular Chaperones / chemistry*
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Molecular Chaperones / metabolism
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Molecular Sequence Data
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Protein Denaturation
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Protein Structure, Secondary
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Sequence Alignment
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Sequence Homology, Amino Acid
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Solvents / chemistry
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Spectrum Analysis
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Thermodynamics
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Titrimetry
Substances
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Haptoglobins
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Heat-Shock Proteins
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Hemoglobins
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Molecular Chaperones
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Solvents
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Catalase