caa a22 4500 397558465 CHVBK 20180308164810.0 cr unu---uuuuu 161202e199611 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021505 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021505 Rat Liver Fatty Acid-Binding Protein: Identification of a Molecular Species Having a Mixed Disulfide with Cysteine at Cysteine-69 and Enhanced Protease Susceptibility [Elektronische Daten] [Tetsuro Sato, Katsuya Baba, Yoshiaki Takahashi, Toshio Uchiumi, Shoji Odani] Fatty acid-binding protein (FABP) has been isolated from rat liver cytosol by two steps of gel-permeation chromatography on Sephadex G-75 and Sephacryl S-100 after ainmonium sulfate precipitation. FABP fraction was eluted as two well-separated peaks, fractions A and B, by reversed-phase high-performance liquid chromatography (HPLC). The structural difference between the two fractions was investigated by lysyl endopeptidase digestion followed by reversed-phase HPLC of the digests, which identified a peptide corresponding to residues 58 through 78 as the modified peptide. Matrix-assisted laserdesorption-ionization mass spectrometry and other chemical analyses of the peptides established the modification in fraction A as cysteine-thiolation at cysteine-69. This was confirmed by reduction and reoxidation of the peptide and the parent molecules. The modification did not affect binding of fluorescent derivatives of fatty acids. However, the modified species was more susceptible to proteolysis by bovine spleen cathepsin B and cathepsin D than the unmodified species. The presence of a relatively large amount of cysteine (but not of glutathione) mixed-disulfide form of FABP suggests some physiological role of this modification related to the redox status of the cell [Thomas, J.A., Poland, B., and Honzatko, R. (1995) Arch. Biochem. Biophys. 319, 1-9], and accounts, at least in part, for the extensive heterogeneity of liver FABP. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence cysteine-thiolation nationallicence fatty acid-binding protein nationallicence mixed disulfide nationallicence post-translational modification nationallicence proteolysis nationallicence Sato Tetsuro Department of Biology, Faculty of Science, Niigata University, Ikarashi Niigata 950-21 aut Baba Katsuya Department of Biology, Faculty of Science, Niigata University, Ikarashi Niigata 950-21 aut Takahashi Yoshiaki Department of Biochemistry, Niigata University school of Medicine Asahimachi, Niigata 951 aut Uchiumi Toshio Department of Biochemistry, Niigata University school of Medicine Asahimachi, Niigata 951 aut Odani Shoji Department of Biology, Faculty of Science, Niigata University, Ikarashi Niigata 950-21 aut The Journal of Biochemistry Oxford University Press 120/5(1996-11), 908-914 0021-924X 120:5<908 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021505 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021505 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Sato Tetsuro Department of Biology, Faculty of Science, Niigata University, Ikarashi Niigata 950-21 aut NATIONALLICENCE 700 1- Baba Katsuya Department of Biology, Faculty of Science, Niigata University, Ikarashi Niigata 950-21 aut NATIONALLICENCE 700 1- Takahashi Yoshiaki Department of Biochemistry, Niigata University school of Medicine Asahimachi, Niigata 951 aut NATIONALLICENCE 700 1- Uchiumi Toshio Department of Biochemistry, Niigata University school of Medicine Asahimachi, Niigata 951 aut NATIONALLICENCE 700 1- Odani Shoji Department of Biology, Faculty of Science, Niigata University, Ikarashi Niigata 950-21 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/5(1996-11), 908-914 0021-924X 120:5<908 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford