scholarly journals EVALUATION OF INDOPHENOL DERIVATIVES AS REAGENTS FOR DEMONSTRATING CYTOCHROME OXIDASE IN TISSUE SECTIONS

1958 ◽  
Vol 6 (6) ◽  
pp. 438-444 ◽  
Author(s):  
DAVID T. CRAWFORD ◽  
MARVIN M. NACHLAS
Keyword(s):  
Cytochrome Oxidase ◽  
Dehydrogenase Activity ◽  
Oxidase Activity ◽  
Succinic Dehydrogenase ◽  
Cytochrome Oxidase Activity ◽  
Tissue Sections ◽  
Enzymatic Action ◽  
Color Fading

Seven redox dyes were investigated as possible histochemical indicators of cytochrome oxidase activity. All failed to meet one prime requisite, namely, that the oxidized product remain at the site of enzymatic action. The "color fading" phenomenon was studied. This effect was one in which sections and homogenates became colored as a result of oxidase activity and then faded during further incubation. Evidence was provided that this reaction occurred as a result of endogenous dehydrogenase activity, mainly succinic dehydrogenase. The decoloration in solution could be prevented by N-ethyl maleimide, without inhibiting cytochrome oxidase.

scholarly journals NONDROPLET ULTRASTRUCTURAL DEMONSTRATION OF CYTOCHROME OXIDASE ACTIVITY WITH A POLYMERIZING OSMIOPHILIC REAGENT, DIAMINOBENZIDINE (DAB)

1968 ◽  
Vol 38 (1) ◽  
pp. 1-14 ◽  
Author(s):  
Arnold M. Seligman ◽  
Morris J. Karnovsky ◽  
Hannah L. Wasserkrug ◽  
Jacob S. Hanker
Keyword(s):  
Cytochrome Oxidase ◽  
Respiratory Chain ◽  
Oxidase Activity ◽  
Oxidative Polymerization ◽  
Succinic Dehydrogenase ◽  
Inner Mitochondrial Membrane ◽  
Electron Microscopic ◽  
Cytochrome Oxidase Activity ◽  
Outer Compartment ◽  
Electron Microscopes

A new method for demonstrating cytochrome oxidase activity, based upon the oxidative polymerization of 3,3'-diaminobenzidine (DAB) to an osmiophilic reaction product, has improved the localization of this enzyme over methods based upon the Nadi reaction, in both the light and electron microscopes. The reaction product occurs in nondroplet form, which more accurately delineates the localization of cytochrome oxidase in mitochondria of heart, liver, and kidney. In electron microscopic preparations the excess reaction product is found to overflow into the intracristate spaces and into the outer compartment between inner and outer limiting mitochondrial membranes. This finding suggests that the enzymatic activity of cytochrome c is located on the inner surface of the intracristate space which is the outer surface of the inner mitochondrial membrane. Succinic dehydrogenase activity has also been located at this site by using an osmiophilic ditetrazolium salt, TC-NBT. Considered together, the sites of reactivity of both parts of the respiratory chain have implications for the chemiosomotic hypothesis of Mitchell who suggests a mechanism of energy conservation during electron transport in the respiratory chain of the mitochondrion.

Cytochrome Oxidase Activity at The Hepatic Parenchyma Different Periods of Ischemia and Obstructive Jaundice

2019 ◽  
Vol 9 (5) ◽  
pp. p8944
Author(s):  
Askarov Tahir Askarovich ◽  
Akhmedov Mirhalil Dzhalilovich ◽  
Fayziev Yokub Nishanovic ◽  
Ashurmetov Ahmadjon Makhamadjonovich ◽  
Dalimov Kenjabek Sabutaevich ◽  
...  
Keyword(s):  
Obstructive Jaundice ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Hepatic Parenchyma ◽  
Cytochrome Oxidase Activity

Histochemical assessment of cytochrome oxidase activity for monitoring ischemic muscle injury

1985 ◽  
Vol 88 (2) ◽  
pp. 265-276 ◽  
Author(s):  
Richard M. Millis ◽  
Theodore A. Stephens ◽  
Gerard Harris ◽  
Columbus Anonye ◽  
Michael Reynolds
Keyword(s):  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Muscle Injury ◽  
Cytochrome Oxidase Activity ◽  
Ischemic Muscle
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