Document Detail

Structural Characterization of Hydroperoxide Lyase in Dodecyl Maltoside by Using Circular Dichroism.
MedLine Citation:
PMID:  23076732     Owner:  NLM     Status:  Publisher    
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.
I Panagakou; E Touloupakis; D F Ghanotakis
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-18
Journal Detail:
Title:  The protein journal     Volume:  -     ISSN:  1875-8355     ISO Abbreviation:  Protein J.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-18     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101212092     Medline TA:  Protein J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Department of Chemistry, University of Crete, P.O. Box 2208, 71003, Voutes-Heraklion, Greece.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  A case of an unusual arrangement of numerous tributaries to the middle temporal vein and its fenestr...
Next Document:  Human ring chromosomes and small supernumerary marker chromosomes-do they have telomeres?