scholarly journals A HISTOCHEMICAL STUDY OF THE LOCALIZATION OF SUCCINIC DEHYDROGENASE, CYTOCHROME OXIDASE AND DIPHOSPHOPYRIDINE NUCLEOTIDE-DIAPHORASE IN THE SYNAPTIC REGIONS OF THE SPINAL CORD IN THE RAT

1964 ◽  
Vol 12 (3) ◽  
pp. 188-193 ◽  
Author(s):  
K. NANDY ◽  
G. H. BOURNE
Keyword(s):  
Spinal Cord ◽  
Cytochrome Oxidase ◽  
Histochemical Study ◽  
Succinic Dehydrogenase

A histochemical study of starch, lipids, and certain enzymes in senescing rose stems

1977 ◽  
Vol 55 (6) ◽  
pp. 617-624 ◽  
Author(s):  
J. M. Molnar ◽  
E. V. Parups
Keyword(s):  
Acid Phosphatase ◽  
Cytochrome Oxidase ◽  
Lipid Content ◽  
Histochemical Study ◽  
Succinic Dehydrogenase ◽  
Sugar Solution ◽  
Lipid Peroxidase ◽  
High Level ◽  
The Rose ◽  
Cut Rose

The starch, lipid, cytochrome oxidase (EC 1.9.3.1), succinic dehydrogenase (EC 1.3.99.1), peroxidase (EC 1.11.1.7), and acid phosphatase (EC 3.1.3.2) levels were determined periodically by histochemical methods in transverse sections of cut stem of the rose, Rosa hybrida L. cv. Forever Yours, kept in water or in an aqueous preservative solution containing 4% sucrose, 100 ppm sodium isoascorbate, and 100 ppm 8-hydroxyquinoline sulfate. Senescence of the cutrose stem, including leaves and flowers, was delayed by use of the sugar solution. The levels of cytochrome oxidase and succinic dehydrogenase were not significantly affected by either of the treatments. Starch, lipid, peroxidase, and acid phosphatase levels decreased in the tissues of rapidly senescing stems kept in water. In tissues where senescence was retarded by use of sugar solutions the lipid content and peroxidase were maintained at a relatively high level; starch, and acid phosphatase levels steadily increased. It is suggested that in cut rose stems, the onset or retardation of senescence is not related to the activities of acid phosphatase or peroxidase.

A histochemical study of the shoot apical meristem of Rauwolfia with reference to differentiation of sclereids

1968 ◽  
Vol 46 (2) ◽  
pp. 115-120 ◽  
Author(s):  
Abdul J. Mia ◽  
Suman M. Pathak
Keyword(s):  
Acid Phosphatase ◽  
Cytochrome Oxidase ◽  
Apical Meristem ◽  
Histochemical Study ◽  
Enzymatic Reaction ◽  
Succinic Dehydrogenase ◽  
Enzyme Systems ◽  
Strong Positive Reaction ◽  
Parenchyma Cells ◽  
Pith Parenchyma

The Rauwolfia apical meristem has three zones which are cytologically recognizable, viz. tunica, corpus, and pith-cell meristem. Histochemically, however, these zonations are not discernible. The entire meristem either reacts positively or negatively for a particular enzyme. The apical meristem and procambial strands give a strong positive reaction for cytochrome oxidase, succinic dehydrogenase, and total protein. The pith cells react positively with peroxidase, acid phosphatase, and phosphorylase. Alkaline phosphatase is distributed throughout the meristematic and non-meristematic areas of the shoot apex. Cells in these areas appear to give slight reaction for glucose-6-phosphatase and 5-nucleotidase. Activities of several enzyme systems, such as cytochrome oxidase, peroxidase, succinic dehydrogenase, and acid phosphatase, were localized in the sclereid initials. Commonly the sclereids give more intensified enzymatic reaction than the pith parenchyma cells.

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.

Sign in / Sign up

Export Citation Format

Share Document