scholarly journals A TETRAZOLIUM SALT REDUCTION METHOD FOR DEMONSTRATING LIPOPROTEINS IN TISSUE SECTIONS

1963 ◽  
Vol 11 (6) ◽  
pp. 738-740 ◽  
Author(s):  
G. G. CARMICHAEL
2013 ◽  
Vol 115 (2) ◽  
pp. 229-232 ◽  
Author(s):  
Damien Michelon ◽  
Sybille Tachon ◽  
Bruno Ebel ◽  
Joëlle De Coninck ◽  
Gilles Feron ◽  
...  

Pharmaceutics ◽  
2022 ◽  
Vol 14 (1) ◽  
pp. 102
Author(s):  
Natalia Zaręba ◽  
Klaudia Więcławik ◽  
Rene Kizek ◽  
Bozena Hosnedlova ◽  
Marta Kepinska

This study aimed to synthesise C60–DOX complexes followed by the analysis of their effect on the concentration of metallothionein (MT) as a non-enzymatic antioxidant and on the concentration and activity of superoxide dismutase (SOD) as an antioxidant enzyme in healthy human mammary MCF-10A cells. Dynamic light scattering and electrophoretic light scattering were used to establish the size and zeta potential of the complexes. The MT and SOD concentrations were determined using the ELISA method; SOD activity was determined by tetrazolium salt reduction inhibition. Lower MT concentration following exposure of cells to both DOX and C60 fullerene compared to the control sample was found. However, the concentration of this protein increased as a consequence of the C60–DOX complexes action on MCF-10A cells compared to the control. C60 used alone did not affect the concentration and activity of SOD in MCF-10A cells. Application of free DOX did not activate cellular antioxidant defence in the form of an increase in SOD concentration or its activity. In contrast treatment of cells with the C60–DOX complex resulted in a decrease in SOD1 concentration and a significant increase in SOD activity compared to cells treated with free DOX, C60 and control. Thus, it was found that C60–DOX complexes showed potential for protective effects against DOX-induced toxicity to MCF-10A cells.


1970 ◽  
Vol 21 (2) ◽  
pp. 170-180 ◽  
Author(s):  
M. J. Eadie ◽  
J. H. Tyrer ◽  
J. R. Kukums ◽  
W. D. Hooper

1958 ◽  
Vol 4 (4) ◽  
pp. 467-474 ◽  
Author(s):  
Marvin M. Nachlas ◽  
Donald G. Walker ◽  
Arnold M. Seligman

A histochemical method is described for the localization of triphosphopyridine nucleotide diaphorase using a recently synthesized tetrazolium salt (Nitro-BT). By virtue of the favorable histochemical properties of this reagent, it has been possible to demonstrate that whereas DPN diaphorase is usually restricted to the mitochondria, the TPN diaphorase activity of corresponding cells was distributed throughout the cytoplasm in granules too fine to be considered mitochondria. Furthermore, although the diaphorase alone is responsible for the passage of electrons from TPNH to the tetrazole, it has been found that sites of activity of different TPN-linked dehydrogenases can be visualized in tissue sections, and characteristic loci for each enzyme may be observed. For example, whereas TPN diaphorase and isocitric dehydrogenase have an extensive distribution in the kidney cortex, 6-phosphogluconic dehydrogenase is limited to the cells of the macula densa.


2019 ◽  
Vol 6 ◽  
Author(s):  
E. Elena García-Martín ◽  
María Aranguren-Gassis ◽  
David M. Karl ◽  
Sandra Martínez-García ◽  
Carol Robinson ◽  
...  

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