Fatty acids bound to recombinant tear lipocalin and their role in structural stabilization.

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.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Tsukamoto S,Fujiwara K,Ikeguchi M

doi

10.1093/jb/mvp076

subject

Has Abstract

pub_date

2009-09-01 00:00:00

pages

343-50

issue

3

eissn

0021-924X

issn

1756-2651

pii

mvp076

journal_volume

146

pub_type

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