S. Odani et al., ON THE MOLECULAR-ORIGIN OF CHARGE HETEROGENEITY OF RAT-LIVER FATTY-ACID-BINDING PROTEIN (Z-PROTEIN), Archives of biochemistry and biophysics, 309(1), 1994, pp. 81-84
The occurrence of many charge isoforms is known for rat liver fatty ac
id-binding protein, and this is the major cause of conflicting data on
the characterization of the protein. Recently, M. Li and T. Ishibashi
(1992, Arch. Biochem. Biophys. 298, 254-258) clearly demonstrated tha
t some charge isoforms are due to bound fatty acids. We found that aci
dic fraction (DE-III) of rat liver fatty acid-binding protein containe
d isoaspartyl-105 protein resulted from deamidation and peptide rearra
ngement at Asn-105. Since DE-III fraction carries mainly arachidonate,
this post-translational modification might modulate binding specifici
ty of fatty acid-binding protein. (C) 1994 Academic Press, Inc.