On the molecular origin of charge heterogeneity of rat liver fatty acid-binding protein (Z-protein).
The occurrence of many charge isoforms is known for rat liver fatty acid-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 that some charge isoforms are due to bound fatty acids. We found that acidic fraction (DE-III) of rat liver fatty acid-binding protein contained isoaspartyl-105 protein resulted from deamidation and peptide rearrangement at Asn-105. Since DE-III fraction carries mainly arachidonate, this post-translational modification might modulate binding specificity of fatty acid-binding protein.
Odani
S
S
Department of Biology, Faculty of Science, Niigata University, Japan.
Okazaki
Y
Y
Kato
C
C
Uchiumi
T
T
Takahashi
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001216:Asparagine / Q000737:chemistry; D001224:Aspartic Acid / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D004563:Electrochemistry; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D008099:Liver / Q000737:chemistry*; D008297:Male; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D051381:Rats; D017208:Rats, Wistar; D012697:Serine Endopeptidases / Q000378:metabolism
D002352:Carrier Proteins; C490174:Fabp7 protein, rat; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D001224:Aspartic Acid; D001216:Asparagine; D012697:Serine Endopeptidases; C036813:lysyl endopeptidase