Protein characterization and fatty acid composition of VHDL subfraction II of the spider Polybetes pythagoricus

VHDL fraction contains hemocyanin as its major apoprotein and transports most of the circulating lipids in the spider Polybetes pythagoricus (Sparassidae). This work shows that subfraction II (the major VHDL component) is composed of a single protein of 420 kDa under native conditions and three subu...

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Detalles Bibliográficos
Autores principales: Laino, Aldana, García, Fernando, Cunningham, Mónica Liliana
Formato: Articulo
Lenguaje:Inglés
Publicado: 2015
Materias:
Bioquímica
Hemocyanin
MALDI-TOF MS
Lipids
Fluorescence
Arachnid
Hexamer
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/104251
http://hdl.handle.net/11336/9064
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-104251
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Bioquímica
Hemocyanin
MALDI-TOF MS
Lipids
Fluorescence
Arachnid
Hexamer
spellingShingle Bioquímica
Hemocyanin
MALDI-TOF MS
Lipids
Fluorescence
Arachnid
Hexamer
Laino, Aldana
García, Fernando
Cunningham, Mónica Liliana
Protein characterization and fatty acid composition of VHDL subfraction II of the spider Polybetes pythagoricus
topic_facet Bioquímica
Hemocyanin
MALDI-TOF MS
Lipids
Fluorescence
Arachnid
Hexamer
description VHDL fraction contains hemocyanin as its major apoprotein and transports most of the circulating lipids in the spider Polybetes pythagoricus (Sparassidae). This work shows that subfraction II (the major VHDL component) is composed of a single protein of 420 kDa under native conditions and three subunits, 67, 105 and 121 kDa under denaturing conditions. Circular dichroism indicated that this subfraction contains 20% α-helix, 29% β-sheet, 22.7% turns and 29.7% unordered structures. Comparison of trypsin susceptibility showed that the 105 and 121 kDa subunits were more susceptible indicating that these proteins would be more exposed to the aqueous medium. Peptide mass fingerprinting of the 67 and 105 kDa subunits indicated the 67 kDa subunit is similar to subunit 3 of the spider Cupiennius salei hemocyanin (21% sequence similarity), whereas the 105 kDa subunit is similar to a protein from the mosquito Anopheles gambiae (20% sequence similarity). The N-terminal amino acid sequence from subunit of 121 kDa was also determined. In relation to fatty acids, 16:0, 18:0, 18:1 and 18:2 were found to be the major components. These data provide a better understanding of VHDL subfraction II structure, which is responsible for most lipid transport in the spider P. pythagoricus.
format Articulo
Articulo
author Laino, Aldana
García, Fernando
Cunningham, Mónica Liliana
author_facet Laino, Aldana
García, Fernando
Cunningham, Mónica Liliana
author_sort Laino, Aldana
title Protein characterization and fatty acid composition of VHDL subfraction II of the spider Polybetes pythagoricus
title_short Protein characterization and fatty acid composition of VHDL subfraction II of the spider Polybetes pythagoricus
title_full Protein characterization and fatty acid composition of VHDL subfraction II of the spider Polybetes pythagoricus
title_fullStr Protein characterization and fatty acid composition of VHDL subfraction II of the spider Polybetes pythagoricus
title_full_unstemmed Protein characterization and fatty acid composition of VHDL subfraction II of the spider Polybetes pythagoricus
title_sort protein characterization and fatty acid composition of vhdl subfraction ii of the spider polybetes pythagoricus
publishDate 2015
url http://sedici.unlp.edu.ar/handle/10915/104251
http://hdl.handle.net/11336/9064
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AT garciafernando proteincharacterizationandfattyacidcompositionofvhdlsubfractioniiofthespiderpolybetespythagoricus
AT cunninghammonicaliliana proteincharacterizationandfattyacidcompositionofvhdlsubfractioniiofthespiderpolybetespythagoricus
bdutipo_str Repositorios
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