Studies on the redox state of cytochrome oxidase in intact rat skeletal muscle (perfused hindlimb) by Dual-Wavelength Spectrophotometry

1982 ◽  
Vol 311 (4) ◽  
pp. 432-433
Author(s):  
P. Schadewaldt ◽  
W. Staib ◽  
P. Graf ◽  
H. Sies
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome Oxidase ◽  
Redox State ◽  
Dual Wavelength ◽  
Rat Skeletal Muscle

scholarly journals Isolation of Relaxing Particles from Rat Skeletal Muscles in Zonal Centrifuges

1965 ◽  
Vol 48 (5) ◽  
pp. 737-752 ◽  
Author(s):  
H. Schuel ◽  
L. Lorand ◽  
R. Schuel ◽  
N. G. Anderson
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Skeletal Muscles ◽  
Microsomal Fraction ◽  
Differential Centrifugation ◽  
Rat Skeletal Muscle ◽  
Cytochrome Oxidase Activity ◽  
Soluble Phase ◽  
Enzymatic Marker

Supernatants of rat skeletal muscle homogenates were fractionated by differential centrifugation and by zonal centrifugation in sucrose density gradients. Cytochrome oxidase was employed as an enzymatic marker for locating mitochondria. The subcellular fractions were also assayed for their ability to prevent the ATP-induced contraction of myofibrils. Both the mitochondrial and microsomal fractions obtained by differential fractionation were found to be rich in such relaxing activity, and the microsomal fraction was appreciably contaminated by mitochondria. In contrast to this, when fractionation was carried out by means of zonal centrifugation (4200 RPM x 205 min. to 40,000 RPM x 60 min.), relaxing activity was found to be associated only with particles having the sedimentation characteristics of microsomes (s20,w estimated to be between 370 and 1880S). Relaxing activity was not detected in the regions of the gradient containing either the starting sample zone (soluble phase) or the mitochondrial peak. The microsomal relaxing particles showed negligible cytochrome oxidase activity.

scholarly journals Is regulation of proteolysis associated with redox-state changes in rat skeletal muscle?

1980 ◽  
Vol 192 (3) ◽  
pp. 963-966 ◽  
Author(s):  
M E Tischler
Keyword(s):  
Skeletal Muscle ◽  
Oxidation State ◽  
Redox State ◽  
Proteinase Activity ◽  
Rat Skeletal Muscle ◽  
Direct Inhibition ◽  
State Changes ◽  
Isolated Rat

In isolated rat diaphragms, only those substrates that increased the tissue NADH/NAD+ ratio lowered the rate of proteolysis. However, direct inhibition of proteinase activity by leupeptin promoted oxidation of the NAD couple of the muscles. These results suggest that changes in muscle reduction-oxidation state may be important in the regulation of proteolysis.

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