INVESTIGADORES
TATIAN Marcos
artículos
Título:
A fatty acid-binding protein and a protein disulphide isomerase-related protein expressed in urochordate gonad cytosol
Autor/es:
CAVAGNARI, B; TATIÁN M; SAHADE R; ESNAL, G; SANTOMÉ, J.A.
Revista:
INTERNATIONAL JOURNAL OF BIOCHEMISTRY AND CELLULAR BIOLOGY
Editorial:
PERGAMON-ELSEVIER SCIENCE LTD
Referencias:
Lugar: Amsterdam; Año: 2000 vol. 32 p. 769 - 777
ISSN:
1357-2725
Resumen:
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