scholarly journals Inhibitory effects of long-chain acyl coenzyme a analogues on rat liver acetyl coenzyme a carboxylase

FEBS Letters ◽  
1979 ◽  
Vol 102 (2) ◽  
pp. 223-226 ◽  
Author(s):  
Jun-ichi Nikawa ◽  
Tadashi Tanabe ◽  
Hideo Ogiwara ◽  
Tetsuo Shiba ◽  
Shosaku Numa
1979 ◽  
Vol 98 (1) ◽  
pp. 165-172 ◽  
Author(s):  
Takao TANAKA ◽  
Kohei HOSAKA ◽  
Minoru HOSHIMARU ◽  
Shosaku NUMA

1965 ◽  
Vol 97 (2) ◽  
pp. 587-594 ◽  
Author(s):  
PB Garland ◽  
D Shepherd ◽  
DW Yates

1. Fluorimetric assays are described for CoASH, acetyl-CoA and long-chain fatty acyl-CoA, and are sensitive to at least 50mumumoles of each. 2. Application of these assays to rat-liver mitochondria oxidizing palmitate in the absence and presence of carnitine indicated two pools of intramitochondrial CoA. One pool could be acylated by palmitate and ATP, and the other pool acylated by palmitate with ATP and carnitine, or by palmitoylcarnitine alone. 3. The intramitochondrial content of acetyl-CoA is increased by the oxidation of palmitate both in the absence and presence of l-malate. 4. The conversion of palmitoyl-CoA into acetyl-CoA by beta-oxidation takes place without detectable accumulation of acyl-CoA intermediates.


Metabolism ◽  
1992 ◽  
Vol 41 (2) ◽  
pp. 201-207 ◽  
Author(s):  
Fernando López-Casillas ◽  
M.Verónica Ponce-Castañeda ◽  
Ki-Han Kim

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