scholarly journals Cytochemical localization of certain oxidative enzymes

1962 ◽  
Vol 110 (1) ◽  
pp. 19-27 ◽  
Author(s):  
James L. Conklin ◽  
Maynard M. Dewey ◽  
Raymond H. Kahn
Keyword(s):  
Oxidative Enzymes ◽  
Cytochemical Localization

scholarly journals THE CYTOCHEMICAL LOCALIZATION OF GLYCOLYTIC AND OXIDATIVE ENZYMES WITHIN MITOCHONDRIA OF SPERMATOZOA OF SOME PULMONATE GASTROPODS

1970 ◽  
Vol 18 (11) ◽  
pp. 783-793 ◽  
Author(s):  
WINSTON A. ANDERSON ◽  
PAUL PERSONNE
Keyword(s):  
Reductase Activity ◽  
Periodic Acid ◽  
Oxidative Enzymes ◽  
Tetrazolium Salt ◽  
Phenazine Methosulfate ◽  
Electron Microscopic ◽  
Cytochemical Localization ◽  
Cytochemical Study ◽  
Mitochondrial Derivative ◽  
The Matrix

In this electron microscopic cytochemical study, the periodic acid-thiosemicarbazide-silver proteinate procedure was used to demonstrate glycogen stores within the mitochondrial derivative of sperm of pulmonate gastropods. In the presence of phenazine methosulfate and tetrazolium salt, enzymatic activity for glyceraldehyde 3-phosphate dehydrogenase and lactate dehydrogenase is shown in the matrix and in the compartment containing glycogen, but in the absence of phenazine methosulfate, tetrazolium reductase activity in the matrix is emphasized. Activity for NADH2-tetrazolium reductase and succinate dehydrogenase is also demonstrated in the matrix. Using 3,3'-diaminobenzidine tetra-HCl, cytochrome c oxidase activity is shown in the paracrystalline mitochondrial structure. The interrelation between glycolytic and oxidative pathways in this highly compartmentalized mitochondrion is considered.

scholarly journals The Cytochemical Localization of Oxidative Enzymes

1958 ◽  
Vol 4 (6) ◽  
pp. 747-752 ◽  
Author(s):  
D. G. Scarpelli ◽  
R. Hess ◽  
A. G. E. Pearse
Keyword(s):  
Cellular Localization ◽  
Oxidative Enzymes ◽  
Tetrazolium Salt ◽  
Direct Transfer ◽  
Metal Chelation ◽  
Cytochemical Localization ◽  
Black Metal ◽  
Respiratory Inhibitors ◽  
Diaphorase Activity ◽  
Tetrazolium Reduction

Cytochemical methods involving metal chelation of the formazan of an N-thiazol-2-yl tetrazolium salt are described for the localization of diphosphopyridine nucleotide diaphorase (DPND) and triphosphopyridine nucleotide diaphorase (TPND) in mitochondria. These methods utilize the reduced coenzymes DPNH or TPNH as substrate. The reaction involves a direct transfer of electrons from reduced coenzyme to the respective diaphorase which in turn transfers the electrons to tetrazolium salt, reducing it to the insoluble formazan. Competition for electrons by preferential acceptors in the respiratory chain was prevented by various inhibitors. In the presence of respiratory inhibitors the rate of tetrazolium reduction was markedly increased. The greatest reduction was observed when amytal was used. Sites of diaphorase activity appeared as deposits of blue-black metal formazan chelate measuring 0.2 to 0.3 µ in diameter. Small mitochondria contained 2 deposits, while larger ones contained up to 6. Considerable differences were observed in the rate of tetrazolium reduction and cellular localization of diaphorase activity when DPNH was used as substrate as compared to TPNH. In each instance DPNH was oxidized more rapidly by tissues than TPNH. These findings support the concept that the oxidation of coenzymes I and II is mediated through separate diaphorases.

CYTOCHEMICAL LOCALIZATION OF TEN OXIDATIVE ENZYMES OF RAT ANTERIOR PITUITARY AND THYROID GLANDS DURING VARIOUS PHASES OF SECRETORY ACTIVITY

1964 ◽  
Vol 29 (1) ◽  
pp. 1-7 ◽  
Author(s):  
H. J. SOBEL
Keyword(s):  
Thyroid Gland ◽  
Anterior Pituitary ◽  
Reductase Activity ◽  
Secretory Activity ◽  
Oxidative Enzymes ◽  
Apparent Difference ◽  
Cytochemical Localization ◽  
Thyroid Glands ◽  
And Migration ◽  
Gonadotrophic Cells

SUMMARY The cytochemical distribution and changes of ten oxidative enzyme systems were studied in rat anterior pituitary and thyroid glands in various phases of secretory activity. Enzyme activity was always localized to discrete, small cytoplasmic particles thought to be mitochondria. Reduced diphosphopyridine nucleotide (DPNH)-Nitro-BT reductase activity in the thyroid gland was also found in nuclear membranes and in cytoplasmic clumps (probably endoplasmic reticulum). There was an apparent increase in number and size and migration toward the Golgi zone of these granules (mitochondria ?) in gonadotrophic cells of castrated rats. No apparent difference was observed in the thyroid gland following thyroxine treatment and exposure to cold.

scholarly journals The Cytochemical Localization of Oxidative Enzymes

1958 ◽  
Vol 4 (6) ◽  
pp. 753-760 ◽  
Author(s):  
R. Hess ◽  
D. G. Scarpelli ◽  
A. G. E. Pearse
Keyword(s):  
Oxidative Enzymes ◽  
Tetrazolium Salt ◽  
Differential Centrifugation ◽  
Mitochondrial Localization ◽  
Cytochemical Localization ◽  
Tissue Sections ◽  
Final Electron ◽  
High Concentrations ◽  
Distinct Distribution ◽  
Final Electron Acceptor

Methods are presented for the intramitochondrial localization of various diphosphopyridine nucleotide and triphosphopyridine nucleotide-linked dehydrogenases in tissue sections. The cytochemical reactions studied involve the oxidation of the substrates by a specific pyridino-protein. The electron transfer of tetrazolium salt is mediated by the diaphorase system associated with the dehydrogenase. The final electron acceptor was either p-nitrophenyl substituted ditetrazole (nitro-BT) or N-thiazol-2-yl monotetrazole (MTT), the latter giving rise to metal formazan in the presence of cobaltous ions. Mitochondrial localization of the formazan precipitate could be achieved by using hypertonic incubating media containing high concentrations of substrate and co-enzyme. A fast reduction of tetrazolium salt was obtained by chemically blocking the respiratory chain enzymes beyond the flavoproteins. Although diaphorase systems are implicated in the reduction of tetrazolium salts, specific dehydrogenases are solely responsible for the distinct distribution pattern obtained in tissues with various substrates. The present findings in tissue sections are discussed in conjunction with existing biochemical evidence from differential centrifugation experiments.

Initial Polymerization Sites Indicated During Mitochondrial Oxidation of Diaminobenzidine after Toluene Treatment

1977 ◽  
Vol 35 ◽  
pp. 408-409
Author(s):  
W. A. Shannon ◽  
M. A. Matlib
Keyword(s):  
Membrane Permeability ◽  
Cytochrome Oxidase ◽  
Rat Liver ◽  
Precise Definition ◽  
Cytochemical Localization ◽  
Oxidative Reaction ◽  
Mitochondrial Oxidation ◽  
Definition Of ◽  
Exogenous Substrates

Numerous studies have dealt with the cytochemical localization of cytochrome oxidase via cytochrome c. More recent studies have dealt with indicating initial foci of this reaction by altering incubation pH (1) or postosmication procedure (2,3). The following study is an attempt to locate such foci by altering membrane permeability. It is thought that such alterations within the limits of maintaining morphological integrity of the membranes will ease the entry of exogenous substrates resulting in a much quicker oxidation and subsequently a more precise definition of the oxidative reaction.The diaminobenzidine (DAB) method of Seligman et al. (4) was used. Minced pieces of rat liver were incubated for 1 hr following toluene treatment (5,6). Experimental variations consisted of incubating fixed or unfixed tissues treated with toluene and unfixed tissues treated with toluene and subsequently fixed.

Peroxidase Localization in Hartmanella Trophozoites

1971 ◽  
Vol 29 ◽  
pp. 346-347 ◽  
Author(s):  
George E. Childs ◽  
Joseph H. Miller
Keyword(s):  
Hydrogen Peroxide ◽  
Ultrastructural Localization ◽  
Pathogenic Strain ◽  
Oxidative Enzymes ◽  
Differential Centrifugation ◽  
Electron Microscopic ◽  
Microscopic Studies ◽  
The Subject ◽  
Axenic Cultures

Biochemical and differential centrifugation studies have demonstrated that the oxidative enzymes of Acanthamoeba sp. are localized in mitochondria and peroxisomes (microbodies). Although hartmanellid amoebae have been the subject of several electron microscopic studies, peroxisomes have not been described from these organisms or other protozoa. Cytochemical tests employing diaminobenzidine-tetra HCl (DAB) and hydrogen peroxide were used for the ultrastructural localization of peroxidases of trophozoites of Hartmanella sp. (A-l, Culbertson), a pathogenic strain grown in axenic cultures of trypticase soy broth.

Cytochemical Localization of Polysaccharides in Diplodia Maydis With Thiosemicarbazide : Evaluation of Three Fixatives For Pa:Tsc:Os Reaction

1976 ◽  
Vol 34 ◽  
pp. 48-49 ◽  
Author(s):  
Judith A. Murphy ◽  
Mary R. Thompson ◽  
A.J. Pappelis
Keyword(s):  
Reaction Center ◽  
Osmium Tetroxide ◽  
Periodic Acid ◽  
Cytochemical Localization ◽  
Thin Sections ◽  
Selective Reaction ◽  
Amorphous Character

In an attempt to identify polysaccharide components in thin sections of D. maydis, procedures were employed such that a PAS localization could be carried out. Three different fixatives were evaluated ie. glutaraldehyde, formaldehyde and paraformaldehyde. These were used in conjunction with periodic acid (PA), thiosemicarbazide(TSC), and osmium tetroxide(Os) to localize polysaccharides in V. maydis using a pre-embedded reaction procedure. Polysaccharide localization is based on the oxidation of vic-glycol groups by PA, and the binding of TSC as a selective reaction center for the formation of osmium black. The reaction product is sufficiently electron opaque, insoluble in lipids, not altered when tissue is embedded, and has a fine amorphous character.

Attenuation of Oxidative Enzymes Induction in Palm Oil Fractions Pre-treated Cadmium Intoxicated Rats

2019 ◽  
Vol 3 (4) ◽  
pp. 107-112 ◽  
Author(s):  
Patrick Ichipi-Ifukor ◽  
Samuel Asagba ◽  
Godfery Kweki ◽  
Chibueze Nwose ◽  
◽  
...  
Keyword(s):  
Palm Oil ◽  
Oxidative Enzymes ◽  
Oil Fractions
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