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- W2053485776 abstract "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." @default.
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- W2053485776 date "1994-02-01" @default.
- W2053485776 modified "2023-09-27" @default.
- W2053485776 title "On the Molecular Origin of Charge Heterogeneity of Rat Liver Fatty Acid-Binding Protein (Z-Protein)" @default.
- W2053485776 doi "https://doi.org/10.1006/abbi.1994.1088" @default.
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