Electron Microscopic Observations on the Sites of Activities of Succinic Dehydrogenase and Cytochrome Oxidase in Mycobacterium tuberculosis and Bacillus megaterium

1966 ◽  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Cytochrome Oxidase ◽  
Bacillus Megaterium ◽  
Succinic Dehydrogenase ◽  
Electron Microscopic

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.

Changes in the cotyledons of Cucurbita maxima during germination. II. Development of mitochondrial function

1970 ◽  
Vol 48 (12) ◽  
pp. 2233-2240 ◽  
Author(s):  
John N. A. Lott ◽  
Paul Castelfranco
Keyword(s):  
Cytochrome Oxidase ◽  
Mitochondrial Function ◽  
Respiratory Activity ◽  
Succinic Dehydrogenase ◽  
Embryo Axis ◽  
Cucurbita Maxima ◽  
Tissue Slices ◽  
Electron Microscopic ◽  
Fresh Tissue ◽  
Microscopic Studies

Mitochondrial respiration in squash cotyledons was followed during germination. Cytochrome oxidase and succinoxidase activities were determined in isolated mitochondrial preparations; tissue localizations of cytochrome oxidase and succinic dehydrogenase were determined histochemically in fresh tissue slices. The respiratory activities differed in light- and dark-germinated plants. In light-grown plants, the respiratory activity reached a peak at 3 days, when the root and the stem were actively growing, and then declined markedly as the tissue became photosynthetic. During the peak, the respiratory activity was present in all the cotyledon tissues; in the foliaceous cotyledons the respiratory activity was localized in the veins. In dark-grown plants the peak of respiratory activity extended over several days and the respiratory rate remained high throughout the cotyledon's life. This broad peak of activity may be related to the mobilization of storage materials for the growth of the embryo axis. In dark-germinated plants, the respiratory activity was widespread throughout the cotyledonary tissues during the peak of activity; the activity became vein localized by 8 days. Electron microscopic studies of cotyledon tissues showed the presence of many mitochondrial profiles in the veinlet regions.

Oxidative Activity of Aortic Tissue of Man, the Rabbit and the Dog, With Special Reference to Succinic Dehydrogenase and Cytochrome Oxidase

1958 ◽  
Vol 195 (2) ◽  
pp. 476-480 ◽  
Author(s):  
Nelicia Maier ◽  
Henry Haimovici
Keyword(s):  
Special Reference ◽  
Cytochrome Oxidase ◽  
Abdominal Aorta ◽  
Abdominal Segment ◽  
Species Difference ◽  
Succinic Dehydrogenase ◽  
Hepatic Tissue ◽  
Human Aorta ◽  
Aortic Tissue ◽  
Enzymatic Systems

Succinic dehydrogenase and cytochrome oxidase activities were determined in homogenates of three aortic segments (ascending and arch, descending thoracic, abdominal) and liver of man, the rabbit and the dog. Both enzymes exhibited the lowest activity in human aorta. Succinic dehydrogenase exhibited the highest activity in the thoracic aorta of the dog and intermediate activity in the latter's abdominal segment and the rabbit's aorta. Cytochrome oxidase, in contrast, exhibited the highest activity in the rabbit's aorta. A slight gradient of decreasing activity from thoracic to abdominal aorta was noted for cytochrome oxidase in both the rabbit and dog and for succinic dehydrogenase in the rabbit, whereas a significant decrease in the latter enzyme was noted in the abdominal segment of the dog. No gradient of activity was apparent in man. Liver exhibited the lowest activity for both enzymes in man, highest in the dog and intermediate in the rabbit. The above findings suggest a biologic species difference between the aorta of man, the rabbit and the dog, which may be partly ascribed to a difference in the components of the above two enzymatic systems. The same species difference holds true for hepatic tissue.

scholarly journals The ultrastructural cytochemistry of lactic dehydrogenase, succinic dehydrogenase, dihydro-nicotinamide adenine dinucleotide diaphorase and cytochrome oxidase activities in hair cell mitochondria of the guinea pig cochlea.

1975 ◽  
Vol 23 (3) ◽  
pp. 216-234 ◽  
Author(s):  
G J Spector
Keyword(s):  
Hair Cell ◽  
Cytochrome Oxidase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Succinic Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Nicotinamide Adenine ◽  
Fixation Method ◽  
Inner Mitochondrial Membrane ◽  
Tetrazolium Chloride ◽  
Outer Compartment

The use of cinnamyl nitroblue tetrazolium chloride (DS-NBT) in dehydrogenase experiments (lactic dehydrogenase, succinic dehydrogenase, nicotinamide adenine dinucleotide diaphorase) and 3,3'-diaminobenzidine tetrahydrochloride (DAB) in cytochrome oxidase experiments indicated that mitochondrial oxidoreduction reactions from nicotinamide adenine dinucleotide to cytochrome oxidase are located on the inner mitochondrial membrane in the outer compartment and the intracristate spaces. These reactions behave according to the chemiosmotic hypothesis. The cochlear hair cell mitochondria are cytochemically indistinguishable from free liver mitochondria. The heterogeneous mitochondrial staining pattern is related to the osmolarity of the incubation media, solubility of the enzymes and pH of the medium, but not to the fixation method.

scholarly journals THE LOCALIZATION OF SUCCINIC DEHYDROGENASE, CYTOCHROME OXIDASE AND ADENOSINE TRIPHOSPHATASE IN CILIATED RESPIRATORY EPITHELIUM

1965 ◽  
Vol 13 (8) ◽  
pp. 677-683 ◽  
Author(s):  
HERTHA R. CRESS ◽  
ALEXANDER SPOCK ◽  
DUNCAN C. HEATHERINGTON
Keyword(s):  
Cytochrome Oxidase ◽  
Adenosine Triphosphatase ◽  
Succinic Dehydrogenase ◽  
Respiratory Epithelium ◽  
Ciliary Activity ◽  
Basal Bodies ◽  
Tissue Cultures ◽  
Respiratory Epithelial Cells ◽  
Respiratory Epithelial

Succinic dehydrogenase and cytochrome oxidase activities were found to be scattered throughout the cytoplasm of ciliated and nonciliated respiratory epithelial cells while ATPase activity was restricted to cilia and areas under the cilia in the regions of the ciliary basal bodies. In order to elucidate the role of ATPase further, tissue cultures of rabbit tracheal epithelium with beating cilia were incubated in a medium perfused with cigarette smoke which resulted in cessation of ciliary motility. Epithelium with beating cilia was positive for ATPase while the epithelium with nonbeating cilia was negative or only weakly positive in a few small scattered areas. The presence of ATPase in beating cilia and its absence in nonbeating cilia agree with biochemical and physiological studies suggesting an association between ATP and ciliary activity.

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