scholarly journals Diurnal variation of cytosolic fatty acid-binding protein content and of palmitate oxidation in rat liver and heart.

1984 ◽  
Vol 259 (7) ◽  
pp. 4295-4300 ◽  
Author(s):  
J F Glatz ◽  
C C Baerwaldt ◽  
J H Veerkamp ◽  
H J Kempen
Keyword(s):  
Fatty Acid ◽  
Diurnal Variation ◽  
Protein Content ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Palmitate Oxidation ◽  
Acid Binding Protein

scholarly journals Intracellular sterol distribution in transfected mouse L-cell fibroblasts expressing rat liver fatty acid-binding protein.

1991 ◽  
Vol 266 (9) ◽  
pp. 5486-5496
Author(s):  
J R Jefferson ◽  
J P Slotte ◽  
G Nemecz ◽  
A Pastuszyn ◽  
T J Scallen ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
L Cell

scholarly journals Effect on ligand binding of arginine mutations in recombinant rat liver fatty acid-binding protein

1994 ◽  
Vol 297 (1) ◽  
pp. 103-107 ◽  
Author(s):  
A E Thumser ◽  
C Evans ◽  
A F Worrall ◽  
D C Wilton
Keyword(s):  
Fatty Acid ◽  
Ligand Binding ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Wide Range ◽  
Arginine Residues

Rat liver fatty acid-binding protein is able to accommodate a wide range of non-polar anions in addition to long-chain fatty acids. The two arginine residues of rat liver fatty acid-binding protein, Arg122 and Arg126, have been mutated and the effect of mutation on ligand binding investigated. No significant decrease in affinity for the fluorescent fatty acid analogue, 11-(5-dimethylaminonaphthalenesulphonyl amino)undecanoic acid, or oleate was observed. However, the apparent affinity for oleoyl-CoA was slightly increased with the mutations Ala122 and Gln122 such that oleoyl-CoA rather than oleate became the preferred ligand for these mutants. Small changes in protein stability were observed with the Arg122 mutations. The lack of notable ionic involvement of the conserved internal residue Arg122 in ligand binding is consistent with the hypothesis that the mode of ligand binding in liver fatty acid-binding protein is markedly different from that of other members of this lipid-binding protein family.

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