The chemical modification of cysteine-69 of rat liver fatty acid-binding protein (FABP): a fluorescence approach to FABP structure and function

1990 ◽  
Vol 98 (1-2) ◽  
Author(s):  
Carol Evans ◽  
DavidC. Wilton
Keyword(s):  
Fatty Acid ◽  
Chemical Modification ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Structure And Function ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
And Function

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

Na pump and plasma membrane structure in L-cell fibroblasts expressing rat liver fatty acid binding protein

1992 ◽  
Vol 298 (1) ◽  
pp. 35-42 ◽  
Author(s):  
Sandra Incerpi ◽  
John R. Jefferson ◽  
W.Gibson Wood ◽  
W.James Ball ◽  
Friedhelm Schroeder
Keyword(s):  
Plasma Membrane ◽  
Fatty Acid ◽  
Rat Liver ◽  
Membrane Structure ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Na Pump

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.

Growth hormone and aging change rat liver fatty acid binding protein levels.

1996 ◽  
Vol 15 (2) ◽  
pp. 169-174 ◽  
Author(s):  
S S Singer ◽  
K Henkels ◽  
A Deucher ◽  
M Barker ◽  
J Singer ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Fatty Acid ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Protein Levels ◽  
Acid Binding Protein ◽  
Aging Change

Fatty acid binding protein isoforms: structure and function

1998 ◽  
Vol 92 (1) ◽  
pp. 1-25 ◽  
Author(s):  
Friedhelm Schroeder ◽  
Christopher A Jolly ◽  
Tae-Hyeon Cho ◽  
Andrey Frolov
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Structure And Function ◽  
Protein Isoforms ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
And Function
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