On the role of oxygen in dehydrogenase reactions using tetrazolium salts

1988 ◽  
Vol 20 (10) ◽  
pp. 587-593 ◽  
Author(s):  
Cornelis J. F. Van Noorden
Keyword(s):  
Tetrazolium Salts

FURTHER OBSERVATIONS ON THE ENZYMATIC REDUCTION OF TETRAZOLIUM SALTS BY MONOAMINES

1958 ◽  
Vol 36 (6) ◽  
pp. 587-594 ◽  
Author(s):  
J. R. Lagnado ◽  
T. L. Sourkes
Keyword(s):  
Rat Liver ◽  
Metal Binding ◽  
Enzyme System ◽  
Enzymatic Reaction ◽  
Free Base ◽  
Tetrazolium Salts ◽  
Enzymatic Reduction ◽  
Tissue Homogenates ◽  
Cofactor Activity

Studies on the role of purines as cofactors in the enzymatic reduction of tetrazolium salts by monoamines have led to the following results: (1) With whole rat liver extracts as the source of enzymes, several purines exhibit cofactor activity either as the free base or as the corresponding riboside and ribotide derivatives. (2) In contrast to this, mitochondrial material from rat liver is active only if adenylic acid or one of several ribotidic derivatives containing an adenylyl or similar moiety is used as cofactor. (3) Mitochondrial material utilizes hypoxanthine as cofactor for the amine/tetrazolium system only in combination with the supernatant obtained by centrifugation of tissue homogenates at 20,000 g. The additional factor present in this supernatant portion is heat-labile and nondialyzable. The possibility that this additional factor is an enzyme or enzymes converting the free base to the ribotide is discussed.Inhibition studies have revealed that the amine/tetrazolium enzyme system is sensitive to several metal-binding agents, but no direct evidence for the role of a metal in the enzymatic reaction could be obtained. It was also found that nicotinamide and adenine, neither of which exhibits cofactor activity, are potent inhibitors of the enzyme system studied.

FURTHER OBSERVATIONS ON THE ENZYMATIC REDUCTION OF TETRAZOLIUM SALTS BY MONOAMINES

1958 ◽  
Vol 36 (1) ◽  
pp. 587-594 ◽  
Author(s):  
J. R. Lagnado ◽  
T. L. Sourkes
Keyword(s):  
Rat Liver ◽  
Metal Binding ◽  
Enzyme System ◽  
Enzymatic Reaction ◽  
Free Base ◽  
Tetrazolium Salts ◽  
Enzymatic Reduction ◽  
Tissue Homogenates ◽  
Cofactor Activity

Studies on the role of purines as cofactors in the enzymatic reduction of tetrazolium salts by monoamines have led to the following results: (1) With whole rat liver extracts as the source of enzymes, several purines exhibit cofactor activity either as the free base or as the corresponding riboside and ribotide derivatives. (2) In contrast to this, mitochondrial material from rat liver is active only if adenylic acid or one of several ribotidic derivatives containing an adenylyl or similar moiety is used as cofactor. (3) Mitochondrial material utilizes hypoxanthine as cofactor for the amine/tetrazolium system only in combination with the supernatant obtained by centrifugation of tissue homogenates at 20,000 g. The additional factor present in this supernatant portion is heat-labile and nondialyzable. The possibility that this additional factor is an enzyme or enzymes converting the free base to the ribotide is discussed.Inhibition studies have revealed that the amine/tetrazolium enzyme system is sensitive to several metal-binding agents, but no direct evidence for the role of a metal in the enzymatic reaction could be obtained. It was also found that nicotinamide and adenine, neither of which exhibits cofactor activity, are potent inhibitors of the enzyme system studied.

The role of oxygen in the reduction of tetrazolium salts with nadh mediated by 5-methyl phenazonium methyl sulfate. An EPR and voltammetric study

1993 ◽  
Vol 19 (7) ◽  
pp. 643-656 ◽  
Author(s):  
P. Carloni ◽  
L. Greci ◽  
E. Maurelli ◽  
P. Stipa ◽  
M. Wozniak ◽  
...  
Keyword(s):  
Methyl Sulfate ◽  
Tetrazolium Salts ◽  
Voltammetric Study

scholarly journals THE REDUCTION OF TETRAZOLIUM SALTS BY ASCITES TUMOR CELLS IN THE PRESENCE OF GLUCOSE

1958 ◽  
Vol 6 (3) ◽  
pp. 174-180 ◽  
Author(s):  
T. BARKA ◽  
G. DALLNER
Keyword(s):  
Tumor Cells ◽  
Ehrlich Ascites Tumor ◽  
Ehrlich Ascites Tumor Cells ◽  
Ascites Tumor ◽  
Electron Carrier ◽  
Tetrazolium Salts ◽  
Qualitative And Quantitative ◽  
Ehrlich Ascites

The Ehrlich ascites tumor cells reduce tetrazolium salts intensely in the presence of glucose. The analysis of this glucose staining indicates the role of an electron-carrier in the glycolysis, probably of glycerolaldehyde-dehydrogenase. The qualitative and quantitative aspects of glucose-staining were investigated and discussed.

Role of dactinomycin in the improved survival of children with Wilms' tumor

JAMA ◽  
1966 ◽  
Vol 195 (12) ◽  
pp. 1005-1009 ◽  
Author(s):  
D. J. Fernbach
Keyword(s):  
Wilms Tumor

Role of the allergist in diagnosis and management of patients with uveitis

JAMA ◽  
1966 ◽  
Vol 195 (3) ◽  
pp. 167-172 ◽  
Author(s):  
T. E. Van Metre
Keyword(s):  
Diagnosis And Management

The power of norms to sway fused group members

2018 ◽  
Vol 41 ◽  
Author(s):  
Winnifred R. Louis ◽  
Craig McGarty ◽  
Emma F. Thomas ◽  
Catherine E. Amiot ◽  
Fathali M. Moghaddam
Keyword(s):  
Evolutionary Anthropology ◽  
Normative Systems ◽  
Violent Extremism ◽  
Identity Fusion ◽  
Group Members

AbstractWhitehouse adapts insights from evolutionary anthropology to interpret extreme self-sacrifice through the concept of identity fusion. The model neglects the role of normative systems in shaping behaviors, especially in relation to violent extremism. In peaceful groups, increasing fusion will actually decrease extremism. Groups collectively appraise threats and opportunities, actively debate action options, and rarely choose violence toward self or others.

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