Journal
PROTEIN JOURNAL
Volume 32, Issue 1, Pages 1-6Publisher
SPRINGER
DOI: 10.1007/s10930-012-9454-1
Keywords
Fatty acid hydroperoxide lyase; Dodecyl maltoside; Secondary structure; Circular dichroism
Categories
Ask authors/readers for more resources
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 % alpha-helix, 32.73 % beta-sheet, 21.76 % turn and 31.13 % unordered.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available