Purification and partial structural characterization of a fatty acid-binding protein from the liver of the South American armadillo Chaetophractus villosus

Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
B M CavagnariJ A Santomé

Abstract

The fatty acid-binding protein (FABP) from armadillo liver was purified to homogeneity by a procedure involving gel filtration and two anion exchange chromatography steps. The purified protein proved to have a pI between 5.0 and 5.2 and migrated by sodium dodecyl sulfate-polyacrilamyde gel electrophoresis as a single entity of approximately 14 kDa. The armadillo FABP cross-reacted with antiserum against rat liver FABP but not against rat intestinal FABP. The same as other members of the family, it has a blocked N-terminus. Amino acid sequencing of peptides obtained by cyanogen bromide cleavage and in-gel tryptic digestion shows that the armadillo, despite being one of the less evolved mammals, has a liver FABP of the same type as that of highly evolved mammals.

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Citations

Jul 24, 1998·The International Journal of Biochemistry & Cell Biology·B M CavagnariJ M Affanni
Oct 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Marcelo D CostabelDiego M A Guérin
May 22, 2001·Archives of Biochemistry and Biophysics·S M Di Pietro, J A Santomé

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