Structural Characterization of Hydroperoxide Lyase in Dodecyl Maltoside by Using Circular Dichroism |
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Authors: | I Panagakou E Touloupakis D F Ghanotakis |
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Institution: | 1. Department of Chemistry, University of Crete, P.O. Box 2208, 71003, Voutes-Heraklion, Greece
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Abstract: | Fatty acid hydroperoxide lyase (HPL) is a membrane protein, member of the lipoxygenase pathway, which holds a central role in plant defense. Green bell pepper fatty acid hydroperoxide lyase, overexpressed in Escherichia coli, was purified and solubilized in two different non ionic detergents, Triton X-100 and dodecyl maltoside (DM). DM is considered to be more useful compared to Triton X-100, as it allows characterization of the protein with spectroscopic techniques, for which Triton X-100 was inapplicable. Circular dichroism demonstrated that HPL’s secondary structure in DM consists of 13.53 % α-helix, 32.73 % β-sheet, 21.76 % turn and 31.13 % unordered. |
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