Presence of two new fatty acid binding proteins in catfish liver

1996 ◽  
Vol 74 (5) ◽  
pp. 675-680 ◽  
Author(s):  
Santiago M. Di Pietro ◽  
José A. Santomé
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Bovine Heart

A basic fatty acid binding protein (FABP), closely related to that of chicken liver, was isolated and characterized from catfish (Rhamdia sapo) liver in a previous work. Results herein show the presence of another two FABPs in which partial amino acid sequences reveal great similarity with the corresponding sequences of other already known FABPs belonging to the heart type. The purification procedures for both proteins involve gel filtration, anion-exchange chromatography, and sodium dodecyl sulfate – polyacrylamide gel electrophoresis (as a last step). Because both FABP N-termini were blocked, they were submitted to in-gel tryptic digestion and the resulting peptides were separated by high performance liquid chromatography, and sequenced by Edman degradation. One of these proteins presented the highest identity percentage when compared with those of the human and bovine heart and bovine brain (81%), and the other when compared with those of chicken retina (75%) and mouse and bovine heart FABP (70%). The presence of several FABPs plus the fact that they belong to different types, as found in the Rhamdia sapo liver, is unusual in mammals, which express a characteristic liver-type member of this protein family.Key words: fatty acid binding protein, liver, catfish, Rhamdia sapo.

Solution structure of bovine heart fatty acid-binding protein (H-FABPC)

1993 ◽  
pp. 15-22
Author(s):  
Dirck Lassen ◽  
Christian Lücke ◽  
Arno Kromminga ◽  
Axel Lezius ◽  
Friedrich Spener ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Solution Structure ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Bovine Heart

scholarly journals Cloning of a full-length complementary DNA for fatty-acid-binding protein from bovine heart

1988 ◽  
Vol 175 (3) ◽  
pp. 549-556 ◽  
Author(s):  
Susanne BILLICHI ◽  
Thomas WISSEL ◽  
Hartmut KRATZIN ◽  
Ulrich HAHN ◽  
Birgit HAGENHOFF ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Full Length ◽  
Fatty Acid Binding ◽  
Complementary Dna ◽  
Acid Binding Protein ◽  
Bovine Heart

scholarly journals Three-dimensional structure of fatty-acid-binding protein from bovine heart

1991 ◽  
Vol 199 (2) ◽  
pp. 271-276 ◽  
Author(s):  
Anke MULLER-FAHRNOW ◽  
Ursula EGNER ◽  
T. Alwyn JONES ◽  
Heinz RUDEL ◽  
Friedrich SPENER ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Fatty Acid Binding ◽  
Three Dimensional Structure ◽  
Acid Binding Protein ◽  
Bovine Heart

scholarly journals Two distinct types of fatty acid-binding protein are expressed in heart ventricle of Antarctic teleost fishes

1998 ◽  
Vol 330 (1) ◽  
pp. 375-382 ◽  
Author(s):  
E. Michael VAYDA ◽  
L. Richard LONDRAVILLE ◽  
E. Robert CASHON ◽  
Lori COSTELLO ◽  
D. Bruce SIDELL
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Cardiac Tissue ◽  
Binding Protein ◽  
Pectoral Muscle ◽  
Amino Acid Sequences ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Gobionotothen Gibberifrons ◽  
Antarctic Teleosts

This report provides the first evidence for the existence of two distinct types of fatty acid-binding protein (FABP) in cardiac tissue of vertebrates. Four species of Antarctic teleost fish (Chaenocephalus aceratus, Cryodraco antarcticus, Gobionotothen gibberifrons and Notothenia coriiceps) exhibited two FABP mRNAs of 1.0 kb and 0.8 kb, which we have termed Hh-FABP and Had-FABP (isolated from eart tissue, with similarity to mammalian eart-type FABP or mammalian ipose-type FABP respectively). These FABP types appear to be products of distinct genes. Both FABP transcripts were abundant in cardiac and aerobic pectoral muscle. However, relative abundance of the two types varied distinctly among other tissues such as kidney, brain, spleen and white muscle. Neither FABP type was expressed in liver or intestine. The coding regions of Hh-FABP and Had-FABP cDNAs from the same species are only ~ 60% identical with one another. However, homologues of each FABP species, which exhibit > 98% identity to their respective types, were isolated from three other Antarctic teleosts. Phylogenetic analysis of aligned amino-acid sequences places Hh-FABP with other vertebrate heart-type FABPs, and Had with adipose/cutaneous FABPs. Expression of two distinct FABPs in cardiac tissue of Antarctic teleosts may be related to their ability to both utilize fatty acid as the primary metabolic fuel and to store lipid intracellularly.

N-terminal variants of fatty acid-binding protein from bovine heart overexpressed in Escherichia coli

1994 ◽  
Vol 33 (3) ◽  
pp. 259-269 ◽  
Author(s):  
Bernfried Specht ◽  
Elke Oudenampsen-Krüger ◽  
Arnd Ingendoh ◽  
Franz Hillenkamp ◽  
Axel G. Lezius ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Bovine Heart

scholarly journals Studies on fatty acid-binding proteins. The diurnal variation shown by rat liver fatty acid-binding protein

1987 ◽  
Vol 242 (3) ◽  
pp. 913-917 ◽  
Author(s):  
T C I Wilkinson ◽  
D C Wilton
Keyword(s):  
Fatty Acid ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Small Variation ◽  
Fatty Acid Binding Proteins ◽  
Peroxisome Proliferator ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

The concentration of fatty acid-binding protein in rat liver was examined by SDS/polyacrylamide-gel electrophoresis, by Western blotting and by quantifying the fluorescence enhancement achieved on the binding of the fluorescent probe 11-(dansylamino)undecanoic acid. A 2-3-fold increase in the concentration of this protein produced by treatment of rats with the peroxisome proliferator tiadenol was readily detected; however, only a small variation in the concentration of the protein due to a diurnal rhythm was observed. This result contradicts the 7-10-fold variation previously reported for this protein [Hargis, Olson, Clarke & Dempsey (1986) J. Biol. Chem. 261, 1988-1991].

scholarly journals The purification and characterization of a fatty acid binding protein specific to pig (Sus domesticus) adipose tissue

1990 ◽  
Vol 267 (2) ◽  
pp. 373-378 ◽  
Author(s):  
M K Armstrong ◽  
D A Bernlohr ◽  
J Storch ◽  
S D Clarke
Keyword(s):  
Adipose Tissue ◽  
Fatty Acid ◽  
Blot Analysis ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Apparent Dissociation Constant ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Western-blot analysis using antiserum to 3T3-L1-cell fatty acid binding protein (FABP) revealed that pig adipose tissue contains a 15 kDa protein immunologically similar to the murine protein. This 15 kDa protein was purified from pig adipose tissue by sequential application of Sephadex G-50 gel filtration, cation exchange and covalent chromatography on Thiol-Sepharose-4B. The purity of the pig protein was established by two-dimensional polyacrylamide-gel electrophoresis. Isoelectric focusing indicated that the pig adipose FABP (a-FABP) exists with two charge isoforms (pI 5.1 and 5.2), both of which persist after delipidation. The N-terminus of the purified pig a-FABP was blocked; however, cleavage with CNBr allowed recovery of a 12-amino-acid peptide which was identical with the murine a-FABP sequence (residues 36-48) at 10 of 12 positions. The pig a-FABP bound 12-(9-anthroyloxy)oleic acid saturably and stoichiometrically, with an apparent dissociation constant of 1.0 microM. Northern-blot analysis using the cDNA for the murine 3T3-L1 FABP revealed that the pig a-FABP was expressed exclusively in adipose tissue.

Expression of fatty acid-binding protein from bovine heart in Escherichia coli

1990 ◽  
pp. 75-79
Author(s):  
Elke Oudenampsen ◽  
Eva-Maria Kupsch ◽  
Thomas Wissel ◽  
Friedrich Spener ◽  
Axel Lezius
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Bovine Heart
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