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Fatty Acids Bound to Recombinant Tear Lipocalin and Their Role in Structural Stabilization
- Source :
- Journal of Biochemistry. 146:343-350
- Publication Year :
- 2009
- Publisher :
- Oxford University Press (OUP), 2009.
-
Abstract
- A variant of human tear lipocalin was expressed in Escherichia coli, and the bound fatty acids were analysed by gas chromatography, mass spectroscopy and nuclear magnetic resonance spectroscopy. Five major fatty acids were identified as hexadecanoic acid (palmitic acid, PA), cis-9-hexadecenoic acid (palmitoleic acid), 9,10-methylenehexadecanoic acid, cis-11-octadecenoic acid (vaccenic acid) and 11,12-methyleneoctadecanoic acid (lactobacillic acid). The composition of the bound fatty acids was similar to the fatty acid composition of E. coli extract, suggesting that the binding affinities are similar for these fatty acids. The urea-induced and thermal-unfolding transitions of the holoprotein (nondelipidated), apoprotein (delipidated) and PA-bound protein were observed by circular dichroism. Holoproteins and PA-bound proteins showed the same stability against urea and heat, and were more stable than apoprotein. These results show that each bound fatty acid stabilizes recombinant tear lipocalin to a similar extent.
- Subjects :
- Cyclopropanes
Protein Denaturation
Hot Temperature
Palmitic Acid
Vaccenic acid
Biochemistry
Gas Chromatography-Mass Spectrometry
Palmitic acid
chemistry.chemical_compound
Escherichia coli
Humans
Transition Temperature
Urea
Palmitoleic acid
Cyclopropane fatty acid
Nuclear Magnetic Resonance, Biomolecular
Molecular Biology
chemistry.chemical_classification
Chromatography
biology
Protein Stability
Circular Dichroism
Fatty Acids
Fatty acid
General Medicine
Recombinant Proteins
chemistry
Spectrophotometry
Fatty Acids, Unsaturated
Free fatty acid receptor
biology.protein
Mutant Proteins
Beta-ketoacyl-ACP synthase
Apoproteins
Ultracentrifugation
Algorithms
Lipocalin 1
Protein Binding
Polyunsaturated fatty acid
Subjects
Details
- ISSN :
- 0021924X
- Volume :
- 146
- Database :
- OpenAIRE
- Journal :
- Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....b981da2966fe981e30bbc4059ee1a937