scholarly journals HISTOCHEMICAL STUDIES OF MITOCHONDRIAL VARIATION DURING AEROBIC GROWTH OF RESPIRATION-NORMAL BAKER'S YEAST

1965 ◽  
Vol 13 (5) ◽  
pp. 344-349 ◽  
Author(s):  
C. J. AVERS ◽  
F. H. LIN ◽  
C. R. PFEFFER
Keyword(s):  
Cytochrome Oxidase ◽  
Succinic Dehydrogenase ◽  
Growth Cycle ◽  
Autonomous Control ◽  
Mitochondrial Enzyme ◽  
Aerobic Growth ◽  
Acceleration Phase ◽  
Enzyme Systems ◽  
Zero Values ◽  
The Common

Histochemical localizations of cytochrome oxidase, succinic dehydrogenase, DPNH-tetrazolium reductase, and TPNH-tetrazolium reductase activities revealed at least two kinds of mitochondria in the intracellular population. The total chondriome in stationary phase cells contains about 45 mitochondria, all with cytochrome oxidase activity. But, only about 30 mitochondria per cell were active for dehydrogenase or reductases. The differences in mitochondrial enzyme activities persisted throughout the growth cycle, showing different numbers of active mitochondria and different rates of their increase and decrease for all four enzyme systems. Manometric data verified the differences between cytochrome oxidase and succinic dehydrogenase for the earlier phases of the growth cycle. In histochemical counts, zero values for all four enzymes occurred in late acceleration phase, but persisted into log phase only for the tetrazolium reductases. Both cytochrome oxidase- and succinic dehydrogenase-active mitochondria began to increase in numbers at the inception of log phase, but at very different rates. The demonstration of more than one kind of mitochondrion in the common nucleocytoplasmic system of a single cell was considered to be evidence of some measure of autonomous control of the mitochondrial phenotype.

scholarly journals MITOCHONDRIAL BIOGENESIS IN NEUROSPORA CRASSA

1971 ◽  
Vol 50 (3) ◽  
pp. 721-736 ◽  
Author(s):  
Neil Howell ◽  
Carol A. Zuiches ◽  
Kenneth D. Munkres
Keyword(s):  
Neurospora Crassa ◽  
Cytochrome Oxidase ◽  
Nuclear Gene ◽  
Nutritional Supplements ◽  
Anaerobic Growth ◽  
Mitochondrial Enzyme ◽  
Aerobic Growth ◽  
Anaerobic Conditions ◽  
New Class ◽  
Obligate Aerobe

The isolation of a new class of mutants permitting facultative anaerobiosis in Neurospora crassa is described. Backcross analyses to the obligate aerobe prototroph (An-) indicate single nuclear gene inheritance (An-/An+). An+ and An- are indistinguishable in morphology and growth rates under aerobic conditions. Anaerobic growth requires nutritional supplements that are dispensable for aerobic growth. Conidiogenesis, conidial germination, and vegetative growth rate are suppressed by anaerobiosis. An+ mutants produce substantial quantities of ethanol under anaerobic conditions. Anaerobiosis and chloramphenicol both affect mitochondrial enzyme activity and morphology. Chloramphenicol inhibition leads to reduction in cytochrome oxidase and swollen mitochondria with few cristae. Anaerobiosis leads to reduction in both cytochrome oxidase and malate dehydrogenase activities, enlarged mitochondria with fewer cristae, enlarged nuclei, and other alterations in cellular morphology. The fine structure of anaerobically grown cells changes with the time of anaerobic growth. We conclude that either inhibition of mitochondrial membrane synthesis or inhibition of respiration might lead to the observed alterations in mitochondria.

Effect of mercuric chloride on some kidney enzymes in chow-fed and sucrose-fed rats

1960 ◽  
Vol 198 (1) ◽  
pp. 187-190 ◽  
Author(s):  
V. Shore ◽  
B. Shore
Keyword(s):  
Alkaline Phosphatase ◽  
Cytochrome Oxidase ◽  
Mercuric Chloride ◽  
Tricarboxylic Acid Cycle ◽  
Succinic Dehydrogenase ◽  
Tricarboxylic Acid ◽  
Acid Cycle ◽  
Enzyme Systems ◽  
Rat Kidneys ◽  
Ketoglutarate Dehydrogenase

Rats given a diet of sucrose and vitamins for 3 weeks or more develop a tolerance to mercuric chloride greater than that of chow-fed rats. Comparison of several enzyme systems (tricarboxylic acid cycle, succinic dehydrogenase, cytochrome oxidase, α-ketoglutarate dehydrogenase, alkaline phosphatase, cathepsins and ß-glucuronidase) in chow-fed and sucrose-fed rats indicated no significant differences in activities. After 3 mg HgCl2/kg i.v., notable differences in the extent of inhibition of tricarboxylic acid enzyme systems were observed. Twenty-four hours after such an injection, kidneys of chow-fed rats were seriously hampered in their ability to perform biological energy transformations. Oxidation and phosphorylation by sucrose-fed rat kidneys were considerably less inhibited.

scholarly journals STUDIES ON THE MECHANISM OF HYDROGEN TRANSPORT IN ANIMAL TISSUES

1943 ◽  
Vol 26 (5) ◽  
pp. 443-455 ◽  
Author(s):  
V. R. Potter ◽  
H. G. Albaum
Keyword(s):  
Alkaline Phosphatase ◽  
Cytochrome C ◽  
Xanthine Oxidase ◽  
Cytochrome Oxidase ◽  
Adenosine Triphosphatase ◽  
Succinic Dehydrogenase ◽  
Hydrogen Transport ◽  
Animal Tissues ◽  
Cytochrome C Reductase ◽  
Enzyme Systems

1. The effect of ribonuclease on various enzyme systems was studied as one approach to the problem of whether or not these enzymes are contained in macromolecules of ribonucleoprotein nature in protoplasm. 2. Ribonuclease inhibited CoI-cytochrome c reductase, succinic dehydrogenase, and cytochrome oxidase, all of which require cytochrome c in order to function. Ribonuclease did not act on cytochrome c. 3. Ribonuclease did not inhibit urease, xanthine oxidase, catalase, alkaline phosphatase, or adenosine triphosphatase under the conditions employed. 4. It was suggested that ribonuclease acted sterically by preventing contact between cytochrome c and its activating centers. 5. It was suggested that the enzymes inhibited may be contained in a ribonucleoprotein of macromolecular dimensions but that the enzymes not inhibited are not necessarily excluded from such a complex by the data presented. 6. Further evidence against the Szent-Györgyi theory of hydrogen transport was presented and discussed.

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.

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