Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites |
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Authors: | Ettrich Rüdiger Brandt Wolfgang Kopecký Vladimír Baumruk Vladimír Hofbauerová Katerina Pavlícek Zdenek |
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Affiliation: | Institute of Physical Biology, Zámek 136, CZ-37333 Nové Hrady, Czech Republic |
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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. |
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