scholarly journals THE EFFECT OF COENZYME Q ON THE HISTOCHEMICAL SUCCINIC TETRAZOLIUM REDUCTASE REACTION: A HISTOCHEMICAL STUDY

1967 ◽  
Vol 15 (4) ◽  
pp. 216-224 ◽  
Author(s):  
CHARLES A. HORWITZ ◽  
LUIS BENITEZ ◽  
MARGARET BRAY

The role played by coenzyme Q (CoQ) in the succinic tetrazolium reductase reaction was investigated. Fresh cryostat sections of normal rat tissues were extracted with acetone to remove CoQ from the tissue sections and the acetone-extracted sections were reconstituted with CoQ-lecithin complexes. The incubation film method for tetrazolium reductases was used as a test system, using succinate as a substrate. Sections from which CoQ had been selectively extracted did not reduce the tetrazolium to its formazan, whereas those acetone-extracted sections that were treated with CoQ-lecithin complexes or with the electron carrier phenazine methosulfate reacted positively. It was concluded that the succinic tetrazolium reductase reaction requires intermediate electron carriers, mainly CoQ. It follows that nitro blue tetrazolium cannot accept electrons directly from the flavins. Therefore, the tetrazolium reductase reaction depends not only on the amount of succinic dehydrogenase and flavins but also on the amount of CoQ in the tissue.

1966 ◽  
Vol 14 (3) ◽  
pp. 254-259 ◽  
Author(s):  
ROGER DAOUST

The substrate film method for localizing RNAse activity has been the object of further studies, and various steps of the original procedure have been modified. The modifications concern mainly the type of RNA used as substrate and the preparation of gelatin-RNA films. Moreover, a technique proposed by other authors for exposing films to tissue sections was found to present interesting advantages and has been adopted. The modified procedure proved more convenient than the original method, and a higher resolution was achieved in the present work. This report describes the revised procedure for localizing RNAse activity in tissue sections, exposes the advantages of the various modifications and presents the results obtained with different rat tissues, namely, the testis, intestine, brain, kidney, pancreas and ovary.


1986 ◽  
Vol 34 (6) ◽  
pp. 827-831 ◽  
Author(s):  
W Hermanns ◽  
F Colbatzky ◽  
A Günther ◽  
B Steiniger

The aim of the present study was to establish a plastic embedding technique that makes possible the immunohistochemical demonstration of class II major histocompatibility complex (MHC) antigens (Ia antigens) in undecalcified joint tissues. Therefore a series of fixatives and dehydrating agents was tested for saving Ia immunoreactivity by post-embedding immunostaining of thin sections (2 microns) of rat tissues that had been embedded in glycol methacrylate (GMA), and by comparing with cryostat sections. An indirect immunoperoxidase and the avidin-biotin complex (ABC) technique were used. Combined with fixation by 4% formaldehyde, dehydration with GMA was found to give the best preservation of Ia antigenicity, followed by dehydration with ethylene glycol. The thinness of tissue sections facilitated the association of Ia antigens with different subcellular compartments in distinct cell populations. These various patterns are described.


1993 ◽  
Vol 264 (4) ◽  
pp. C995-C1002 ◽  
Author(s):  
W. T. Monacci ◽  
M. J. Merrill ◽  
E. H. Oldfield

Vascular permeability factor (VPF)/vascular endothelial growth factor (VEGF) is a approximately 43-kDa secreted protein that has been shown in bioassays to induce endothelial proliferation, angiogenesis, and capillary hyperpermeability. VPF has been suggested to play an important role in the physiology of normal vasculature. To further elucidate the natural functions of VPF in vivo, the expression of VPF in normal tissues was examined using Northern blot analysis and in situ hybridization histochemistry. VPF mRNA is expressed in the brain, kidney, liver, lung, and spleen of the healthy adult rat. On Northern blots, the relative abundance of VPF mRNA observed in these tissues was highest in the lung and lowest in the spleen. As determined by in situ hybridization, the patterns of VPF expression are organ specific. Hybridization of an antisense VPF probe was concentrated in the cerebellar granule cell layer of the brain and in the glomeruli and tubules of the kidney. In the liver and lung, intense hybridization was observed homogeneously throughout both tissues, demonstrating that VPF mRNA is present in virtually every hepatocyte and pulmonary alveolar cell. Hybridization to the spleen was weaker and more diffuse. The widespread expression and organ-specific distribution of VPF mRNA in normal rat tissues supports the suggestion of an extensive role for this factor in the physiology of normal vasculature.


PROTOPLASMA ◽  
2003 ◽  
Vol 221 (1-2) ◽  
pp. 11-17 ◽  
Author(s):  
C. G�mez-D�az ◽  
M. I. Bur�n ◽  
F. J. Alca�n ◽  
R. Gonz�lez-Ojeda ◽  
J. A. Gonz�lez-Reyes ◽  
...  

1958 ◽  
Vol 6 (6) ◽  
pp. 438-444 ◽  
Author(s):  
DAVID T. CRAWFORD ◽  
MARVIN M. NACHLAS

Seven redox dyes were investigated as possible histochemical indicators of cytochrome oxidase activity. All failed to meet one prime requisite, namely, that the oxidized product remain at the site of enzymatic action. The "color fading" phenomenon was studied. This effect was one in which sections and homogenates became colored as a result of oxidase activity and then faded during further incubation. Evidence was provided that this reaction occurred as a result of endogenous dehydrogenase activity, mainly succinic dehydrogenase. The decoloration in solution could be prevented by N-ethyl maleimide, without inhibiting cytochrome oxidase.


Sign in / Sign up

Export Citation Format

Share Document