Journal
HIGH PRESSURE RESEARCH
Volume 31, Issue 1, Pages 243-252Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/08957959.2010.543900
Keywords
static and dynamic light scattering; protein complexes; ligand binding; intermolecular interactions
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Funding
- Deutsche Forschungsgemeinschaft [FR 456/25-4, A1+A4]
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The high pressure dissociation of hemocyanin prepared from the lobster Homarus americanus and casein micelles from cow milk were observed by in situ light scattering. The hemocyanin dodecamer dissociated via a hexamer into monomers in a two-step three-species reaction. The influence of ligands and the effector l-lactate on the dissociation behavior was investigated. While no effect by carbon monoxide after exchanging the ligand oxygen was observed, the addition of the effector l-lactate led to a decrease in the pressure stability. Due to a trimer intermediate which was found to be stabilized by l-lactate, the dissociation reaction in the presence of the effector was analyzed by a three-step four-species reaction. In the case of casein micelles, a two-step dissociation mechanism was found. The stabilizing interactions of casein micelles were identified and separated.
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