Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Odani, S.
Right arrow Articles by Takahashi, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Odani, S.
Right arrow Articles by Takahashi, Y.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 2001, Vol. 129, No. 1 69-76
© 2001 Japanese Biochemical Society


other

Hepatic Fatty Acid-Binding Proteins of a Teleost, Lateolabrax japonicus. The Primary Structures and Location of a Disulfide Bond1

Shoji Odani*,2, Katsuya Baba*, Yutaka Tsuchida*, Yutaka Aoyagi{dagger}, Shuji Wakui{ddagger} and Yoshiaki Takahashi§

*Department of Biology, Faculty of Science, Niigata University Ikarashi, Niigata 950-2181
{dagger}Department of Internal Medicine III, School of Medicine, Faculty of Medicine, Niigata University Asahimachi, Niigata 951-8122
{ddagger}Department of Physiology, School of Medicine, Faculty of Medicine, Niigata University Asahimachi, Niigata 951-8122
§Department of Medical Technology, School of Health Science, Faculty of Medicine, Niigata University Asahimachi, Niigata 951-8122

2To whom correspondence should be addressed. Tel: +81-25-262-6174, Fax: +81-25-262-6116, E-mail: sodani{at}sc.niigata-u.ac.jp

Two fatty acid-binding proteins (FABP), FABP-1 and FABP-2, were purified from the liver cytosol of the teleost, Lateolabrax japonicus (Japan sea bass), and characterized. The complete primary structure of FABP-2 was determined by protein analysis to be the following: MDFSGTWQVY AQENYEEFLR AMELPADVIK MAKDIKPITE IKQSGNDFVV TSKTPGKTVT NSFTIGKEAD ITTMDGKKIR CVVNLEGGKL VCNTGKFCHI QELRGGEMVE TLTMGSTTLI RKSKKM. Partial peptide sequences of FABP-1 were also determined. Phylogenetic analysis indicates that FABP-2 is a homologue of mammalian hepatic FABP, whereas FABP-1 is most similar to the members of mammalian cardiac FABP subfamily. L. japonicus FABP-2 contains three cysteine residues, and a disulfide bond is identified between Cys-81 and Cys-92. A theoretical model of FABP-2 generated by a homology modeling method indicates close proximity of the two cysteine residues in the three-dimensional structure. This is a rather rare case of cytosolic protein having a disulfide bond under the normally reducing conditions of the cytosol, though the presence or absence of disulfide bonds does not seem to affect the ligand-binding ability.

1This research was supported by a Grant-in-Aid for Scientific Research (C-10680579) from the Ministry of Education, Science, Sports and Culture of Japan.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
S. Capaldi, M. Guariento, G. Saccomani, D. Fessas, M. Perduca, and H. L. Monaco
A Single Amino Acid Mutation in Zebrafish (Danio rerio) Liver Bile Acid-binding Protein Can Change the Stoichiometry of Ligand Binding
J. Biol. Chem., October 19, 2007; 282(42): 31008 - 31018.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.