Purification of carnitine acetyltransferase from skeletal muscle of the camel (Camelus dromedarius)

1996 ◽  
Vol 165 (2) ◽  
Author(s):  
A.S. Alhomida ◽  
A.S. Duhaiman ◽  
A.A. Al-Jafari ◽  
M.A. Junaid
Keyword(s):  
Skeletal Muscle ◽  
Camelus Dromedarius ◽  
Carnitine Acetyltransferase

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 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.

scholarly journals A carnitine/acylcarnitine translocase assay applicable to biopsied muscle specimens without requiring mitochondrial isolation

1986 ◽  
Vol 236 (1) ◽  
pp. 143-148 ◽  
Author(s):  
M S R Murthy ◽  
V S Kamanna ◽  
S V Pande
Keyword(s):  
Skeletal Muscle ◽  
Rat Heart ◽  
Skeletal Muscles ◽  
Human Skeletal Muscle ◽  
Carnitine Acetyltransferase ◽  
Fresh Tissue ◽  
Simple Method ◽  
Oxidase System ◽  
Acylcarnitine Translocase ◽  
Mitochondrial Transporters

A simple method for assaying the mitochondrial carnitine/acylcarnitine translocase of muscles that needs only few milligrams of fresh tissue is described. The procedure involves monitoring of the sulphobetaine (an inhibitor of the translocase)-sensitive acetylation of sub-saturating concentrations of carnitine in the medium, linked to the oxidation of [2-14C]pyruvate in the presence of malonate. Conditions affecting the reliability of the outlined procedure and the ancillary information to be collected, namely the activities of pyruvate oxidase system and carnitine acetyltransferase, for detecting possible deficiency of the translocase are described, together with data on the translocase activity in human skeletal muscle, in rat red and white skeletal muscles and in rat heart. The concepts outlined should allow development of assays of other mitochondrial transporters that also would require neither isolation of mitochondria nor availability of a large quantity of tissue, both of which are otherwise needed at present.

Endotoxin Alteration of the Mucopolysaccharide Blood Vessel Coating in Rats

1974 ◽  
Vol 32 ◽  
pp. 148-149
Author(s):  
D. E. Philpott ◽  
A. Takahashi
Keyword(s):  
Skeletal Muscle ◽  
Endothelial Cells ◽  
Salivary Gland ◽  
Carotid Artery ◽  
Basement Membrane ◽  
Coronary Vessels ◽  
Ruthenium Red ◽  
E Coli ◽  
Old Rats ◽  
The Brain

Two month, eight month and two year old rats were treated with 10 or 20 mg/kg of E. Coli endotoxin I. P. The eight month old rats proved most resistant to the endotoxin. During fixation the aorta, carotid artery, basil arartery of the brain, coronary vessels of the heart, inner surfaces of the heart chambers, heart and skeletal muscle, lung, liver, kidney, spleen, brain, retina, trachae, intestine, salivary gland, adrenal gland and gingiva were treated with ruthenium red or alcian blue to preserve the mucopolysaccharide (MPS) coating. Five, 8 and 24 hrs of endotoxin treatment produced increasingly marked capillary damage, disappearance of the MPS coating, edema, destruction of endothelial cells and damage to the basement membrane in the liver, kidney and lung.

Ultra-Rapid Freezing of Isolated Skeletal Muscle Fibers

1977 ◽  
Vol 35 ◽  
pp. 576-577
Author(s):  
Joachim R. Sommer ◽  
Nancy R. Wallace
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Granular Material ◽  
Nuclear Envelope ◽  
Intracellular Calcium ◽  
Ruthenium Red ◽  
Threshold Concentration ◽  
Rapid Freezing ◽  
Frog Skeletal Muscle ◽  
Electrical Isolation

After Howell (1) had shown that ruthenium red treatment of fixed frog skeletal muscle caused collapse of the intermediate cisternae of the sarcoplasmic reticulum (SR), forming a pentalaminate structure by obi iterating the SR lumen, we demonstrated that the phenomenon involves the entire SR including the nuclear envelope and that it also occurs after treatment with other cations, including calcium (2,3,4).From these observations we have formulated a hypothesis which states that intracellular calcium taken up by the SR at the end of contraction causes the M rete to collapse at a certain threshold concentration as the first step in a subsequent centrifugal zippering of the free SR toward the junctional SR (JSR). This would cause a) bulk transport of SR contents, such as calcium and granular material (4) into the JSR and, b) electrical isolation of the free SR from the JSR.

Electron Probe Analysis of Muscle

1982 ◽  
Vol 40 ◽  
pp. 398-401
Author(s):  
A. V. Somlyo ◽  
H. Shuman ◽  
A. P. Somlyo
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Sarcoplasmic Reticulum ◽  
Resting State ◽  
Binding Sites ◽  
Electron Probe ◽  
Frog Skeletal Muscle ◽  
Electron Probe Analysis ◽  
Probe Analysis

Electron probe analysis of frozen dried cryosections of frog skeletal muscle, rabbit vascular smooth muscle and of isolated, hyperpermeab1 e rabbit cardiac myocytes has been used to determine the composition of the cytoplasm and organelles in the resting state as well as during contraction. The concentration of elements within the organelles reflects the permeabilities of the organelle membranes to the cytoplasmic ions as well as binding sites. The measurements of [Ca] in the sarcoplasmic reticulum (SR) and mitochondria at rest and during contraction, have direct bearing on their role as release and/or storage sites for Ca in situ.

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