Fatty acids bound to <Emphasis Type="Italic">Fasciola hepatica</Emphasis> 12 kDa fatty acid-binding protein,a candidate vaccine,differ from fatty acids in extracts of adult flukes |
| |
Authors: | Email author" target="_blank">Néstor?M?CarballeiraEmail author Heidyleen?Cruz George?V?Hillyer |
| |
Affiliation: | (1) Department of Pathology and Laboratory Medicine, School of Medicine, University of Puerto Rico Medical Sciences Campus, 00936-5067 San Juan, Puerto Rico;(2) Dept. of Chemistry, University of Puerto Rico, P.O. Box 23346 San Juan, Puerto Rico, 00931-3346 |
| |
Abstract: | The FA composition of Fasciola hepatica 12 kDA purified native FA-binding protein (nFh12), a candidate vaccine against fascioliasis, is described. The FA chain lengths ranged between 12 and 24 carbons. The
principal FA were 16∶0 18∶1n−9, 18∶0, 20∶4n−6, and 20∶1n−9. The acids 16∶0, 18∶1n−9, and 18∶0 comprised over half the FA that
were bound to the whole FA-binding protein. Small amounts (1.0–2.8%) of isoanteiso methyl-branched FA also were characterized. Forty-one different FA were identified in extracts of the adult flukes, with
the three most abundant FA also being 16∶0, 18∶1n−9, and 18∶0. A similar proportion of saturated vs. unsaturated FA was observed
between the whole extract from F. hepatica and the nFh12 protein. However, the n−3/n−6 ratio of PUFA was significantly different, being 1.2 in the whole extract vs. 9.6 in the
nFh12 protein complex. The nFh12 protein binds more n−5, n−6, and n−7 PUFA and less n−3 and n−9 PUFA than the whole extract. In addition, cholesterol
(56%), sitosterol (36%), and fucosterol (8%) also were bound to the nFh12 protein complex. |
| |
Keywords: | |
本文献已被 PubMed SpringerLink 等数据库收录! |
|