scholarly journals Inhibition studies of the carnitine acetyltransferase from skeletal muscle of the camel (Camelus dromedarius) by sulfhydryl reagents and metal ions

IUBMB Life ◽  
1996 ◽  
Vol 39 (5) ◽  
pp. 923-931 ◽  
Author(s):  
AS Alhomida
Keyword(s):  
Skeletal Muscle ◽  
Metal Ions ◽  
Camelus Dromedarius ◽  
Carnitine Acetyltransferase ◽  
Sulfhydryl Reagents ◽  
Inhibition Studies

Kinetic properties of purified carnitine acetyltransferase from the skeletal muscle of Arabian camel (Camelus dromedarius)

Biochimie ◽  
1996 ◽  
Vol 78 (3) ◽  
pp. 204-208 ◽  
Author(s):  
A.S. Alhomida ◽  
A.A. Al-Jafari ◽  
A.S. Duhaiman ◽  
N. Rabbani ◽  
M.A. Junaid
Keyword(s):  
Skeletal Muscle ◽  
Camelus Dromedarius ◽  
Kinetic Properties ◽  
Carnitine Acetyltransferase ◽  
Arabian Camel

scholarly journals Carnitine acetyltransferase: A new player in skeletal muscle insulin resistance?

2017 ◽  
Vol 9 ◽  
pp. 47-50 ◽  
Author(s):  
Sofia Mikkelsen Berg ◽  
Henning Beck-Nielsen ◽  
Nils Joakim Færgeman ◽  
Michael Gaster
Keyword(s):  
Insulin Resistance ◽  
Skeletal Muscle ◽  
Carnitine Acetyltransferase ◽  
Muscle Insulin Resistance ◽  
Skeletal Muscle Insulin Resistance

scholarly journals Synthesis, Characterization, Molecular Docking and Enzyme Inhibition Studies of Some Novel Enaminone Derivatives and Their Complexes with Cu(II), Cd(II) and Co(II) Ions

2019 ◽  
Vol 70 (10) ◽  
pp. 3564-3569
Author(s):  
Rahila Huma ◽  
Tariq Mahmud ◽  
Liviu Mitu ◽  
Muhammad Ashraf ◽  
Ambar Iqbal ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Transition Metal ◽  
Metal Ions ◽  
Metal Complexes ◽  
1H Nmr ◽  
13C Nmr ◽  
Transition Metal Ions ◽  
Binding Mode ◽  
Inhibitory Activities ◽  
Inhibition Studies

Two new enaminone ligands, 3-chloro-4-{(4-chlorophenyl)amino}pent-3-en-2-one (Ac-PCA), 4-(benzylamino)-3-chloropent-3-en-2-one (Ac-BA) and their metal complexes with transition metal ions [Cu(II), Cd(II) and Co(II)] were prepared and subsequently characterized by FTIR, ICP-AES, UV-Vis, TGA, 1H NMR, 13C NMR and FAB-MS. These newly synthesized compounds were further investigated for anti-acetylcholinesterase (AChE) and anti-urease activities. The (Ac-BA)Cu(II) complex exhibited good anti-AChE while (Ac-BA)2Co(II) complex was potent against anti-urease activities. Other ligands and complexes showed poor to no enzyme inhibitory activities. The synthesized compounds were docked inside acetylcholinesterase enzymes to determine their putative binding mode.

Effect of Metal Ions, EDTA and Sulfhydryl Reagents on Soybean Amylase Activity

2011 ◽  
Vol 6 (3) ◽  
pp. 282-290 ◽  
Author(s):  
Om Prakash ◽  
Nivedita Jaiswal ◽  
Rajesh Kumar Pand
Keyword(s):  
Metal Ions ◽  
Amylase Activity ◽  
Sulfhydryl Reagents

scholarly journals Relationships between carnitine and coenzyme A esters in tissues of normal and alloxan-diabetic sheep

1972 ◽  
Vol 127 (1) ◽  
pp. 133-141 ◽  
Author(s):  
A. M. Snoswell ◽  
Patricia P. Koundakjian
Keyword(s):  
Skeletal Muscle ◽  
Alloxan Diabetes ◽  
Biceps Femoris ◽  
Kidney Cortex ◽  
Carnitine Acetyltransferase ◽  
Total Acid ◽  
Acetyl Coa ◽  
Adult Sheep ◽  
Ruminant Metabolism

1. The total acid-soluble carnitine concentrations of four tissues from Merino sheep showed a wide variation not reported for other species. The concentrations were 134, 538, 3510 and 12900nmol/g wet wt. for liver, kidney cortex, heart and skeletal muscle (M. biceps femoris) respectively. 2. The concentration of acetyl-CoA was approximately equal to the concentration of free CoA in all four tissues and the concentration of acid-soluble CoA (free CoA plus acetyl-CoA) decreased in the order liver>kidney cortex>heart>skeletal muscle. 3. The total amount of acid-soluble carnitine in skeletal muscle of lambs was 40% of that in the adult sheep, whereas the concentration of acid-soluble CoA was 2.5 times as much. A similar inverse relationship between carnitine and CoA concentrations was observed when different muscles in the adult sheep were compared. 4. Carnitine was confined to the cytosol in all four tissues examined, whereas CoA was equally distributed between the mitochondria and cytosol in liver, approx. 25% was present in the cytosol in kidney cortex and virtually none in this fraction in heart and skeletal muscle. 5. Carnitine acetyltransferase (EC 2.3.1.7) was confined to the mitochondria in all four tissues and at least 90% of the activity was latent. 6. Acetate thiokinase (EC 6.2.1.1) was predominantly (90%) present in the cytosol in liver, but less than 10% was present in this fraction in heart and skeletal muscle. 7. In alloxan-diabetes, the concentration of acetylcarnitine was increased in all four tissues examined, but the total acid-soluble carnitine concentration was increased sevenfold in the liver and twofold in kidney cortex. 8. The concentration of acetyl-CoA was approximately equal to that of free CoA in the four tissues of the alloxan diabetic sheep, but the concentration of acid-soluble CoA in liver increased approximately twofold in alloxan-diabetes. 9. The relationship between CoA and carnitine and the role of carnitine acetyltransferase in the various tissues is discussed. The quantitative importance of carnitine in ruminant metabolism is also emphasized.

Acetyl-1-14C-l-carnitine Oxidation, Carnitine Acetyltransferase Activity, and CoA Content in Skeletal Muscle Mitochondria from Normal and Dystrophic Mice (Strain 129)

1972 ◽  
Vol 50 (7) ◽  
pp. 749-754 ◽  
Author(s):  
J. J. Jato-Rodriguez ◽  
C. H. Lin ◽  
A. J. Hudson ◽  
K. P. Strickland
Keyword(s):  
Skeletal Muscle ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
Carnitine Acetyltransferase ◽  
Dystrophic Muscle ◽  
Mitochondrial Content ◽  
Acid Cycle ◽  
Skeletal Muscle Mitochondria ◽  
Leg Muscle ◽  
Dystrophic Mice

Mitochondria isolated from the hind leg muscle of normal and dystrophic mice (strain 129) were compared in their capacity to oxidize acetyl-1-14C-l-carnitine. Oxidation in the mitochondria from dystrophic animals was reduced by 80%. Carnitine acetyltransferase (EC 2.3.1.7) activity in the mitochondria was determined and showed a 35% reduction in the mitochondria from dystrophic muscle. A larger decrease (55%) was observed in the mitochondrial content of acid-soluble CoA. Although the combined decreases in carnitine acetyltransferase and CoA can largely account for the observed decrease in acetylcarnitine oxidation in the mitochondria isolated from dystrophic muscle, it is conceivable that some defect may still exist in the utilization of acetyl groups in the tricarboxylic acid cycle.

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