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Hysteresis on Heating and Cooling of E. coli Alkaline Phosphatase

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Measurements of [θ]222 of E. coli phosphatase on heating from 20° to 90° and subsequent cooling to 20° shows a gradual increase in [θ]222 on heating, while cooling shows a symmetric transition centered at 45°. Reheating and cooling shows the same phenomenon. Enzyme heated and cooled once is fully active. The activity of the enzyme depends on its storage conditions (buffer and pH for example), but such changes are least to some extent reversible, especially by heating in different solvents. We conclude the enzyme exists in several forms which are in slow equilibrium with each other, so that the enzyme responds slowly when heated and hence is not at equilibrium during heating/cooling experiments.

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Keywords: Alkaline phosphatase; circular dichroism (CD) profile; differential scanning calorimetry (DSC); nonequilibrium; subunit association; thermal hysteresis

Document Type: Research Article

Publication date: June 1, 2008

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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