id paper:paper_13572725_v32_n7_p769_Cavagnari
record_format dspace
spelling paper:paper_13572725_v32_n7_p769_Cavagnari2023-06-08T16:11:15Z A fatty acid-binding protein and a protein disulphide isomerase-related protein expressed in urochordate gonad cytosol Fatty acid-binding proteins Molgula pedunculata Protein disulphide isomerase Sequence comparison Urochordates actin binding protein fatty acid binding protein palmitic acid protein disulfide isomerase adipocyte amino acid sequence article cytosol enzyme activity gonad nonhuman protein analysis protein binding protein expression species differentiation Amino Acid Sequence Animals Cytosol Fatty Acid-Binding Proteins Gastrointestinal Tract Gonads Humans Molecular Sequence Data Protein Disulfide-Isomerases Sequence Alignment Urochordata Ascidia Invertebrata Molgula pedunculata Pedunculata Urochordata Vertebrata Despite the evolutionary-tree data suggesting that gene duplication leading to the divergence of the three branches which heart, liver and intestinal fatty acid-binding proteins belong to must have occurred before the vertebrate/invertebrate split, only the heart fatty acid-binding protein has been reported for invertebrates. In an attempt to shed light on this apparent inconsistency the presence of the other two branch members was investigated in the Urochordata Molgula pedunculata, an ascidian species close to vertebrates. The mantle-, gonad- and digestive tube-cytosolic fractions, obtained by centrifugation at 106,000 g, were incubated separately with [1-14C]palmitic acid and then fractionated on a Sephadex G-75 column. In the case of gonads and digestive tube, radioactive peaks corresponding to a molecular mass of 14-16 kDa, characteristic of fatty acid-binding proteins, were detected. When the experiment was performed on the mantle, this peak showing fatty acid binding capacity was absent. Western Blot of the radioactive 14-16 kDa Sephadex fraction from the urochordate gonad cross- reacted with rat liver fatty acid-binding protein anti-serum but did not do so with anti-rat intestinal, adipocyte or heart fatty acid-binding protein antisera. The material from the digestive tube was not recognized by any of the antisera. The most abundant protein in said 14-16 kDa fraction was a protein disulphide isomerase-related protein. Its partial amino acid sequence was determined. (C) 2000 Elsevier Science Ltd. 2000 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13572725_v32_n7_p769_Cavagnari http://hdl.handle.net/20.500.12110/paper_13572725_v32_n7_p769_Cavagnari
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Fatty acid-binding proteins
Molgula pedunculata
Protein disulphide isomerase
Sequence comparison
Urochordates
actin binding protein
fatty acid binding protein
palmitic acid
protein disulfide isomerase
adipocyte
amino acid sequence
article
cytosol
enzyme activity
gonad
nonhuman
protein analysis
protein binding
protein expression
species differentiation
Amino Acid Sequence
Animals
Cytosol
Fatty Acid-Binding Proteins
Gastrointestinal Tract
Gonads
Humans
Molecular Sequence Data
Protein Disulfide-Isomerases
Sequence Alignment
Urochordata
Ascidia
Invertebrata
Molgula pedunculata
Pedunculata
Urochordata
Vertebrata
spellingShingle Fatty acid-binding proteins
Molgula pedunculata
Protein disulphide isomerase
Sequence comparison
Urochordates
actin binding protein
fatty acid binding protein
palmitic acid
protein disulfide isomerase
adipocyte
amino acid sequence
article
cytosol
enzyme activity
gonad
nonhuman
protein analysis
protein binding
protein expression
species differentiation
Amino Acid Sequence
Animals
Cytosol
Fatty Acid-Binding Proteins
Gastrointestinal Tract
Gonads
Humans
Molecular Sequence Data
Protein Disulfide-Isomerases
Sequence Alignment
Urochordata
Ascidia
Invertebrata
Molgula pedunculata
Pedunculata
Urochordata
Vertebrata
A fatty acid-binding protein and a protein disulphide isomerase-related protein expressed in urochordate gonad cytosol
topic_facet Fatty acid-binding proteins
Molgula pedunculata
Protein disulphide isomerase
Sequence comparison
Urochordates
actin binding protein
fatty acid binding protein
palmitic acid
protein disulfide isomerase
adipocyte
amino acid sequence
article
cytosol
enzyme activity
gonad
nonhuman
protein analysis
protein binding
protein expression
species differentiation
Amino Acid Sequence
Animals
Cytosol
Fatty Acid-Binding Proteins
Gastrointestinal Tract
Gonads
Humans
Molecular Sequence Data
Protein Disulfide-Isomerases
Sequence Alignment
Urochordata
Ascidia
Invertebrata
Molgula pedunculata
Pedunculata
Urochordata
Vertebrata
description Despite the evolutionary-tree data suggesting that gene duplication leading to the divergence of the three branches which heart, liver and intestinal fatty acid-binding proteins belong to must have occurred before the vertebrate/invertebrate split, only the heart fatty acid-binding protein has been reported for invertebrates. In an attempt to shed light on this apparent inconsistency the presence of the other two branch members was investigated in the Urochordata Molgula pedunculata, an ascidian species close to vertebrates. The mantle-, gonad- and digestive tube-cytosolic fractions, obtained by centrifugation at 106,000 g, were incubated separately with [1-14C]palmitic acid and then fractionated on a Sephadex G-75 column. In the case of gonads and digestive tube, radioactive peaks corresponding to a molecular mass of 14-16 kDa, characteristic of fatty acid-binding proteins, were detected. When the experiment was performed on the mantle, this peak showing fatty acid binding capacity was absent. Western Blot of the radioactive 14-16 kDa Sephadex fraction from the urochordate gonad cross- reacted with rat liver fatty acid-binding protein anti-serum but did not do so with anti-rat intestinal, adipocyte or heart fatty acid-binding protein antisera. The material from the digestive tube was not recognized by any of the antisera. The most abundant protein in said 14-16 kDa fraction was a protein disulphide isomerase-related protein. Its partial amino acid sequence was determined. (C) 2000 Elsevier Science Ltd.
title A fatty acid-binding protein and a protein disulphide isomerase-related protein expressed in urochordate gonad cytosol
title_short A fatty acid-binding protein and a protein disulphide isomerase-related protein expressed in urochordate gonad cytosol
title_full A fatty acid-binding protein and a protein disulphide isomerase-related protein expressed in urochordate gonad cytosol
title_fullStr A fatty acid-binding protein and a protein disulphide isomerase-related protein expressed in urochordate gonad cytosol
title_full_unstemmed A fatty acid-binding protein and a protein disulphide isomerase-related protein expressed in urochordate gonad cytosol
title_sort fatty acid-binding protein and a protein disulphide isomerase-related protein expressed in urochordate gonad cytosol
publishDate 2000
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13572725_v32_n7_p769_Cavagnari
http://hdl.handle.net/20.500.12110/paper_13572725_v32_n7_p769_Cavagnari
_version_ 1768544097129201664