Search PubMed⌕ Search

Biomedical subjects

C D Seufert

Publications and source records attributed to C D Seufert.

9 recordsLinked to original sources
PubMed1984

Effect of long-term starvation on acetate and ketone body metabolism in obese patients.

The turnover of ketone bodies and acetate was evaluated as well from the disappearance rate of (3-14C)acetoacetate or (1-14C)acetate respectively as from the conversion of FFA into these metabolites in normal weight and obese overnight-fasted and in obese long-term starved patients. The disappearance rate of (1-14C)oleate was the same in all three groups. Long-term starvation enhanced ketone body turn-over almost 10-fold, whereas the disappearance rate for ketone bodies decreased from 0.035 to 0.015 min-1. Under the same circumstances the turnover of acetate was about 1 mumol g-1 min-1 accounting for about 5% of FFA turnover. Long-term starvation decreased the conversion of (1-14C)oleate into triglycerides by almost 50% and increased the (2-C)-(4-C)/(1-C) ratio of radioactivity in ketone bodies. The reincorporation of radioactivity from the (1-C)position of (1-14C)oleate into the ( (2-C)-(n-C) ) position of FFA, which is a measure of the reutilization of acetyl-CoA for FFA synthesis decreased significantly during long-term starvation.

3-Hydroxybutyric Acid↗
PubMed1979

Acetyl-coenzyme A deacylase activity in liver is not an artifact. Subcellular distribution and substrate specificity of acetyl-coenzyme A deacylase activities in rat liver.

Whole liver and isolated liver mitochondria are able to release free acetate, especially under conditions of increased fatty acid oxidation. In the present paper it is shown that rat liver contains acetyl-CoA deacylase (EC 3.1.2.1) activity (0.72mumol/min per g wet wt. of liver at 30 degrees C and 0.5mm-acetyl-CoA). At 0.5mm-acetyl-CoA 73% of total enzyme activity was found in the mitochondria, 8% in the lysosomal fraction and 19% in the postmicrosomal supernatant. Mitochondrial subfractionation shows that mitochondrial acetyl-CoA deacylase activity is restricted to the matrix space. Mitochondrial acetyl-CoA deacylase showed almost no activity with either butyryl- or hexanoyl-CoA. Acetyl-CoA hydrolase activity from purified rat liver lysosomes exhibited a very low affinity for acetyl-CoA (apparent K(m)>15mm compared with an apparent K(m) value of 0.5mm for the mitochondrial enzyme) and reacted at about the same rate with acetyl-, n-butyryl- and hexanoyl-CoA. We could not confirm the findings of Costa & Snoswell [(1975) Biochem. J.152, 167-172] according to which mitochondrial acetyl-CoA deacylase was considered to be an artifact resulting from the combined actions of acetyl-CoA-l-carnitine acetyltransferase (EC 2.3.1.7) and acetylcarnitine hydrolase. The results are in line with the concept that free acetate released by the liver under physiological conditions stems from the intramitochondrial deacylation of acetyl-CoA.

Acetyl-CoA Hydrolase↗