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Palmitate oxidation was measured in muscle homogenates using a modified method of that described by Turner et al. [38].
The pH was determined in the muscle homogenates using a combination pH electrode (Model FC200 Hanna Instruments, Leighton Buzzard, UK).
Concentration of ubiquitinated myosin and total myosin were determined as described before in whole diaphragm muscle homogenates, using standard Western blotting [ 4, 16].
CaN activity was determined in skeletal muscle homogenates using the BIOMOL CaN cellular assay kit plus (Enzo Life Sciences Ltd ,Exeter, UK).
Protein oxidation was evaluated through protein carbonyl content in skeletal muscle homogenates using Protein carbonyl Assay kit (CAYMAN Chemical, Ann Arbor, MI, USA) according to the manufacturer's instructions.
Content of myosin heavy chain (MyHC) was analyzed in diaphragm muscle homogenates using standard Western blotting as described previously [ 4, 16].
Similar(53)
The myofibrillar and sarcoplasmic protein-fractions were separated from a muscle homogenate using a common solubility/centrifugation procedure [16].
Increased MVI content was also observed in denervated soleus muscle homogenate using western blot (Fig. 1b).
Citrate synthase activity was measured from whole muscle homogenate using the spectrophotometric method published by Srere [ 19].
Total RNA extracted from the muscle tissues, homogenated using the TRIzol/choloroform/isopropanol method followed by the removal of supernatants.
Frozen-thawed mitochondrial isolates and powdered whole muscle homogenates were used in Western blotting experiments to determine the relative amounts of each of the electron transport chain complexes in isolated mitochondria.
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