PURIFICATION AND PARTIAL STRUCTURAL CHARACTERIZATION OF A FATTY-ACID-BINDING PROTEIN FROM THE LIVER OF THE SOUTH-AMERICAN ARMADILLO CHAETOPHRACTUS-VILLOSUS

The fatty acid-binding protein (FABP) from armadillo liver was purifie d 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-polyacri lamyde gel electrophoresis as a single entity of approximately 14 kDa. The armadillo FABP cross-reacted with antiserum against rat liver FAB P but not against rat intestinal FABP. The same as other members of th e family, it has a blocked N-terminus. Amino acid sequencing of peptid es obtained by cyanogen bromide cleavage and in-gel tryptic digestion shows that the armadillo, being one of the less evolved mammals, has a liver FABP of the same type as that of highly evolved mammals. (C) 19 97 Elsevier Science Inc.