scholarly journals HISTOCHEMICAL DEMONSTRATION OF CYTOCHROME OXIDASE WITH NEW AMINE REAGENTS

1960 ◽  
Vol 8 (1) ◽  
pp. 63-70 ◽  
Author(s):  
M. S. BURSTONE
1964 ◽  
Vol s3-105 (72) ◽  
pp. 497-502
Author(s):  
R. G. BUTCHER ◽  
J. V. DIENGDOH ◽  
J. CHAYEN

Burstone's procedure for the histochemical demonstration of cytochrome oxidase has been studied and applied to sections prepared by freezing in hexane and cutting by the controlled-temperature freezing-sectioning technique. The method has been modified by the inclusion of a treatment with Lugol's iodine to yield a stronger colour, which is stable for at least several weeks and which localizes the enzyme activity more precisely. The variants of the reaction have been compared in their effect on cardiac muscle, liver, and kidney of the rat.


1978 ◽  
Vol 26 (3) ◽  
pp. 157-162 ◽  
Author(s):  
A C Frasch ◽  
M E Itoiz ◽  
R L Cabrini

Polyacrylamide models in which an extract of cattle heart mitochondria was incorporated, as well as cryostat sections of tongue muscle and epithelium, were used to set up the conditions under which the histochemical reaction for the demonstration of cytochrome oxidase can be quantitated. Using diaminobenzidine in a concentration of 5.5 mM, cytochrome C in a fixed concentration of 76 micron and keeping the incubation medium away from direct light action, enzyme activity can be evaluated by means of direct microphotometry on tissue sections. Each biologic model requires previous individual determination of the measurement limits. These limits can be readily established by using a small chamber for the incubation medium, which can be placed in the microphotometer, allowing the reaction rate to be following using a single section.


1958 ◽  
Vol 6 (6) ◽  
pp. 445-456 ◽  
Author(s):  
MARVIN M. NACHLAS ◽  
DAVID T. CRAWFORD ◽  
THEODORE P. GOLDSTEIN ◽  
ARNOLD M. SELIGMAN

By synthesizing an analogue of N,N-dimethyl-p-phenylene diamine, a new reagent for the Nadi reaction was found which provided a useful histochemical method for either cytochrome oxidase (G-Nadi) or peroxidase (M-Nadi). The new agent is 4-amino-1-N,N-dimethylnaphthylamine and yields with α-naphthol, an indonaphthol purple pigment which is more stable and more satisfactorily distributed in tissue than the indophenol blue of the Nadi reaction. Thin sections may be used, some permanence of color is obtained and the granules are fine and anatomically distributed. The localization of cytochrome oxidase activity in heart, stomach, spleen, and cerebellum of the rat is described.


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