Biochemical verification of quantitative histochemical analysis of succinate dehydrogenase activity in skeletal muscle fibres

1993 ◽  
Vol 25 (7) ◽  
pp. 491-496 ◽  
Author(s):  
Scott K. Powers ◽  
Fu-Kong Lieu ◽  
David Criswell ◽  
Stephen Dodd
Keyword(s):  
Skeletal Muscle ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Muscle Fibres ◽  
Histochemical Analysis ◽  
Succinate Dehydrogenase Activity ◽  
Skeletal Muscle Fibres

Intracellular distribution of succinate dehydrogenase activity in skeletal muscle fibers of geese

1984 ◽  
Vol 62 (2) ◽  
pp. 235-240 ◽  
Author(s):  
H. J. Swatland
Keyword(s):  
Skeletal Muscle ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Adenosine Triphosphatase ◽  
Muscle Fibers ◽  
Fiber Types ◽  
Succinate Dehydrogenase Activity ◽  
Individual Muscle ◽  
Concentric Zone ◽  
Pectoralis Muscles

Samples of iliotibialis anterior and pectoralis muscles were taken from five ganders (Anser domesticus). Serial transverse sections were reacted for succinate dehydrogenase (SDH) and alkali-stable adenosine triphosphatase (ATPase). The distribution of SDH activity within individual muscle fibers was measured with a scanning photometer. In many individual fibers, SDH activity was stronger in the periphery than in the axis. This gradient was steepest (−0.034 ± 0.019 absorbance units per concentric zone of 2 μm diameter measurements) in pectoralis fibers with strong SDH activity. In the pectoralis, radial gradients were correlated with fiber area so that the smallest fibers tended to have the steepest gradients of SDH activity. However, this relationship was reversed in fibers with strong ATPase and weak SDH activity in the iliotibialis anterior, and the largest fibers tended to have the steepest gradients. In all fiber types of both muscles, fibers with greater mean SDH activity tended to have steeper gradients.

scholarly journals Assay of succinate dehydrogenase activity by the tetrazolium method: evaluation of an improved technique in skeletal muscle fractions.

1980 ◽  
Vol 28 (5) ◽  
pp. 408-412 ◽  
Author(s):  
J D Green ◽  
H T Narahara
Keyword(s):  
Skeletal Muscle ◽  
Ethyl Acetate ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Inhibitory Effects ◽  
Succinate Dehydrogenase Activity ◽  
Low Concentrations ◽  
Mitochondrial Fractions ◽  
Mitochondrial Suspension ◽  
Improved Technique

An improved spectrophotometric method for measuring succinate dehydrogenase (EC 1.3.99.1) activity with the use of 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride (INT) is described. The procedure has been evaluated in mitochondrial fractions and homogenates of frog skeletal muscle. For mitochondrial suspensions, extraction of formazan with alcohol was found to be superior to extraction with ethyl acetate. For homogenates, complete extraction of formazan required sequential treatment with alcohol and ethyl acetate; the generally employed procedure of extracting once with ethyl acetate alone led to serious underestimation of the amount of formazan in the tissue. Observations of mitochondrial suspension incubated with various concentrations of INT led to the selection of 0.8 mM INT for optimal results. Higher concentrations, although commonly used, can exert undesirable inhibitory effects on succinate dehydrogenase activity, especially at low concentrations of mitochondria and after longer periods of incubation. The problem of instability of succinate dehydrogenase was solved by the addition of buffer at pH 7.5.

Sign in / Sign up

Export Citation Format

Share Document