Cavagnari B M, Córdoba O L, Affanni J M, Santomé J A
Instituto the Química y Fisicoquímica Biológicas (IQUIFIB)-CONICET-UBA, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Argentina.
Comp Biochem Physiol B Biochem Mol Biol. 1997 Sep;118(1):173-80. doi: 10.1016/s0305-0491(97)00052-7.
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.
