scholarly journals Quantitation of hepatic fatty acid-binding proteins by post-chromatographic ligand binding assay

1983 ◽  
Vol 24 (3) ◽  
pp. 324-331
Author(s):  
F D Morrow ◽  
R J Martin
1990 ◽  
Vol 265 (3) ◽  
pp. 849-855 ◽  
Author(s):  
J T Rasmussen ◽  
T Börchers ◽  
J Knudsen

Bovine and rat liver acyl-CoA-binding proteins (ACBP) were found to exhibit a much higher affinity for long-chain acyl-CoA esters than both bovine hepatic and cardiac fatty-acid-binding proteins (hFABP and cFABP respectively). In the Lipidex 1000- as well as the liposome-binding assay, bovine and rat hepatic ACBP effectively bound long-chain acyl-CoA ester, h- and c-FABP were, under identical conditions, unable to bind significant amounts of long-chain acyl-CoA esters. When FABP, ACBP and [1-14C]hexadecanoyl-CoA were mixed, hexadecanoyl-CoA could be shown to be bound to ACBP only. The experimental results give strong evidence that ACBP, and not FABP, is the predominant carrier of acyl-CoA in liver.


1987 ◽  
Vol 242 (3) ◽  
pp. 919-922 ◽  
Author(s):  
M Sheridan ◽  
T C I Wilkinson ◽  
D C Wilton

The concentration of hepatic fatty acid-binding protein was determined in the livers of rats at various stages of development from foetus to young adult. Fatty acid-binding protein concentrations were determined by quantifying the fluorescence enhancement on the binding of the fluorescent probe 11-(dansylamino)-undecanoic acid. A 20-fold increase in the concentration of the protein was observed between the foetus and adult, and this increase was confirmed by immuno-blotting. No other protein in the 14,000-Mr range was observed in the foetus. Possible alternative fatty acid-binding proteins could not be detected in h.p.l.c.-fractionated foetal cytosol by the fluorescence-enhancement method.


1986 ◽  
Vol 88 (S2) ◽  
pp. 588-592 ◽  
Author(s):  
U. Bordewick ◽  
H. Schulenberg ◽  
P. Schäfer ◽  
F. Spener

1984 ◽  
Vol 259 (21) ◽  
pp. 13395-13401 ◽  
Author(s):  
P Brecher ◽  
R Saouaf ◽  
J M Sugarman ◽  
D Eisenberg ◽  
K LaRosa

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