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dc.contributor.author
Pasquevich, María Yanina  
dc.contributor.author
Dreon, Marcos Sebastian  
dc.contributor.author
Lavarias, Sabrina Maria Luisa  
dc.contributor.author
Heras, Horacio  
dc.date.available
2017-09-21T21:31:37Z  
dc.date.issued
2011-08-26  
dc.identifier.citation
Pasquevich, María Yanina; Dreon, Marcos Sebastian; Lavarias, Sabrina Maria Luisa; Heras, Horacio; Triacylglycerol catabolism in the prawn Macrobrachium borellii (Crustacea: Palaemoniade); Elsevier Science; Comparative Biochemistry And Physiology. Part B, Biochemistry & Molecular Biology.; 160; 4; 26-8-2011; 201-207  
dc.identifier.issn
1096-4959  
dc.identifier.uri
http://hdl.handle.net/11336/24893  
dc.description.abstract
While invertebrates store neutral lipids as their major energy source, little is known about triacylglycerol (TAG) class composition and their differential catabolism in aquatic arthropods. This study focuses on the composition of the main energy source and its catabolism by lipase from the midgut gland (hepatopancreas) of the crustacean Macrobrachium borellii. Silver-ion thin-layer chromatography of prawn large TAG deposit (80% of total lipids) and its subsequent fatty acid analysis by gas chromatography allowed the identification of 4 major fractions. These are composed of fatty acids of decreasing unsaturation and carbon chain length, the predominant being 18:1n-9. Fraction I, the most unsaturated one, contained mainly 20:5n-3; fraction II 18:2n-6; fraction III 18:1n-9 while the most saturated fraction contained mostly 16:0. Hepatopancreas main lipase (Mr 72 kDa) cross-reacted with polyclonal antibodies against insect lipase, was not dependent on the presence of Ca2+ and had an optimum activity at 40 °C and pH 8.0. Kinetic analysis showed a Michaelis? Menten behavior. A substrate competition assay evidenced lipase specificity following the order: 18:1n- 9-TAGNPUFA-enriched-TAGN16:0-TAG different from that in vertebrates. These data indicate there is a reasonable correspondence between the fatty acid composition of TAG and the substrate specificity of lipase, which may be an important factor in determining which fatty acids are mobilized during lipolysis for oxidation in crustaceans.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier Science  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Lipase  
dc.subject
Triacylglycerol  
dc.subject
Lipid Metabolism  
dc.subject
Crustacean  
dc.subject.classification
Bioquímica y Biología Molecular  
dc.subject.classification
Ciencias Biológicas  
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS  
dc.title
Triacylglycerol catabolism in the prawn Macrobrachium borellii (Crustacea: Palaemoniade)  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2017-09-19T14:35:36Z  
dc.journal.volume
160  
dc.journal.number
4  
dc.journal.pagination
201-207  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Amsterdam  
dc.description.fil
Fil: Pasquevich, María Yanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata ; Argentina. Universidad Nacional de la Plata. Facultad de Ciencias Médicas; Argentina  
dc.description.fil
Fil: Dreon, Marcos Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata ; Argentina. Universidad Nacional de la Plata. Facultad de Ciencias Médicas; Argentina  
dc.description.fil
Fil: Lavarias, Sabrina Maria Luisa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Limnología "Dr. Raúl A. Ringuelet". Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Instituto de Limnología; Argentina. Universidad Nacional de la Plata. Facultad de Ciencias Médicas; Argentina  
dc.description.fil
Fil: Heras, Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata ; Argentina  
dc.journal.title
Comparative Biochemistry And Physiology. Part B, Biochemistry & Molecular Biology.  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1096495911001734  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.cbpb.2011.08.006