Cavagnari B M, Córdoba O L, Veerkamp J H, Santomé J A, Affanni J M
Instituto de Química y Fisicoquímica Biológicas (IQUIFIB)-CONICET-UBA, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Argentina.
Int J Biochem Cell Biol. 1998 Apr;30(4):465-73. doi: 10.1016/s1357-2725(98)00013-2.
A fatty acid-binding protein from the cytosolic fraction of the armadillo Chaetophractus villosus Harderian gland was purified to homogeneity by a procedure based on gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The protein has an apparent molecular mass of 14 kDa. N-terminal sequence analysis showed that the protein has a blocked N-terminus. For internal amino acid sequencing, the protein was digested in-gel and the resulting peptides were fractionated by reverse-phase high performance liquid chromatography and subjected to automated Edman degradation. Partial amino acid sequencing suggests that it belongs to the heart type. Moreover, it cross-reacted with anti-serum to rat heart fatty acid-binding protein but not with rat intestinal and liver anti-sera. A very slow cross-reaction was also found with anti-serum to rat ALBP. This is the first time that a fatty acid-binding protein has been reported in a Harderian gland.
