Histochemical localization of mushroom tyrosinase in whole tissue sections on nitrocellulose

1989 ◽  
Vol 90 (5) ◽  
pp. 379-381 ◽  
Author(s):  
B. M. Moore ◽  
B. Kang ◽  
W. H. Flurkey
Keyword(s):  
Histochemical Localization ◽  
Mushroom Tyrosinase ◽  
Tissue Sections

scholarly journals Localization of Peroxidase in Grapes using Nitrocellulose Blotting of Freezing/Thawing Fruits

HortScience ◽  
1993 ◽  
Vol 28 (1) ◽  
pp. 38-40 ◽  
Author(s):  
Antonio A. Calderón ◽  
Jose M. Zapata ◽  
Romualdo Muñoz ◽  
A. Ros Barceló
Keyword(s):  
Vitis Vinifera ◽  
Vascular Bundle ◽  
Peroxidase Activity ◽  
Histochemical Localization ◽  
Vascular Bundles ◽  
Reaction Products ◽  
Tissue Sections ◽  
Bundle Structure

A technique has been developed to study the histochemical localization of peroxidase in Vitis vinifera by blotting freezing/thawing tissue sections on nitrocellulose membranes. After being stained with 4-methoxy- α -naphthol and H2O2, peroxidase-mediated reaction products in mature `Gamay' grapes were seen principally in the skin and, to a lesser extent, the pericarp, where discrete areas of reaction products were located in the vascular bundles. However, for immature `Gamay' and `Grenache' grapes, peroxidase activity in the skin was low and similar to that found in the pericarp. With this technique, fruit vascular bundle structure was preserved. The reliability of the technique in the histochemical localization of peroxidase in grapes was confirmed by fractionation and determining the peroxidase activity in the various tissues.

scholarly journals Histochemical Localization of Dehydrogenases in Tissue Sections

1962 ◽  
Vol 1962 (3) ◽  
pp. 36-38
Author(s):  
Kensaku KAWAKATSU ◽  
Tuneo MIZUSHIMA ◽  
Kinji YOSHIKAWA ◽  
Masahiko MORI
Keyword(s):  
Histochemical Localization ◽  
Tissue Sections

scholarly journals The Histochemical Localization of Triphosphopyridine Nucleotide Diaphorase

1958 ◽  
Vol 4 (4) ◽  
pp. 467-474 ◽  
Author(s):  
Marvin M. Nachlas ◽  
Donald G. Walker ◽  
Arnold M. Seligman
Keyword(s):  
Macula Densa ◽  
Histochemical Method ◽  
Histochemical Localization ◽  
Kidney Cortex ◽  
Tetrazolium Salt ◽  
Tissue Sections ◽  
Isocitric Dehydrogenase ◽  
Diaphorase Activity

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.

scholarly journals MODIFIED PROCEDURE FOR THE HISTOCHEMICAL LOCALIZATION OF RIBONUCLEASE ACTIVITY BY THE SUBSTRATE FILM METHOD

1966 ◽  
Vol 14 (3) ◽  
pp. 254-259 ◽  
Author(s):  
ROGER DAOUST
Keyword(s):  
Original Method ◽  
Ribonuclease Activity ◽  
Rnase Activity ◽  
Histochemical Localization ◽  
Rat Tissues ◽  
Tissue Sections ◽  
Original Procedure ◽  
Film Method ◽  
Substrate Film

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.

scholarly journals Selective histochemical localization of polysaccharides in tissue sections oxidized by acetic anhydride in dimethyl sulfoxide.

1976 ◽  
Vol 24 (9) ◽  
pp. 993-999 ◽  
Author(s):  
G I Malinin
Keyword(s):  
Acetic Anhydride ◽  
Dimethyl Sulfoxide ◽  
Ribonucleic Acid ◽  
Deoxyribonucleic Acid ◽  
Acid Hydrazide ◽  
Color Reaction ◽  
Histochemical Localization ◽  
Tissue Sections ◽  
Naphthoic Acid

Oxidation of tissue sections by 25-30% (v/v) acetic anhydride (AA) in dimethyl sulfoxide (DMSO) resulted in facile induction of tissue carbonyls readily localized with Schiff's reagent and o-dianisidine but not with the 3-hydroxy-2-naphthoic acid hydrazide-tetraazotized diorthoanisidine method. Carbonyls generated by AA-DMSO oxidation were confined predomintly to substrates containing pyranosides. Oxidized furanosides, as represented by deoxyribonucleic acid and ribonucleic acid, gave only a residual color reaction. The AA-DMSO method possesses an advantage in that the oxidation of tissue polysaccharides does not proceed beyond the formation of carbonyly and is particularly suited for use after formol fixation.

Histochemical Localization of T-Cells in Tissue Sections

1979 ◽  
Vol 23 (4) ◽  
pp. 886 ◽  
Author(s):  
S. Odend'hal ◽  
E. C. Player
Keyword(s):  
T Cells ◽  
Histochemical Localization ◽  
Tissue Sections

The Application of Protein A-Gold Immunocytochemistry to Studies of Protein Secretion

1985 ◽  
Vol 43 ◽  
pp. 426-429
Author(s):  
George H. Herbener ◽  
Antonio Nanci ◽  
Moise Bendayan
Keyword(s):  
Tissue Section ◽  
Colloidal Gold ◽  
Unit Area ◽  
Protein A ◽  
Extracellular Proteins ◽  
Gold Complex ◽  
Second Step ◽  
Igg Antibodies ◽  
Tissue Sections ◽  
Antigenic Sites

Protein A-gold immunocytochemistry is a two-step, post-embedding labeling procedure which may be applied to tissue sections to localize intra- and extracellular proteins. The key requisite for immunocytochemistry is the availability of the appropriate antibody to react in an immune response with the antigenic sites on the protein of interest. During the second step, protein A-gold complex is reacted with the antibody. This is a non- specific reaction in that protein A will combine with most IgG antibodies. The ‘label’ visualized in the electron microscope is colloidal gold. Since labeling is restricted to the surface of the tissue section and since colloidal gold is particulate, labeling density, i.e., the number of gold particles per unit area of tissue section, may be quantitated with ease and accuracy.

Discovery of intracellular 2,8 dihydroxyadenine crystals in bovine lymphatic and hepatic cells

1987 ◽  
Vol 45 ◽  
pp. 906-907
Author(s):  
W. E. Rigsby ◽  
D. M. Hinton ◽  
V. J. Hurst ◽  
P. C. McCaskey
Keyword(s):  
Polarized Light ◽  
Paraffin Sections ◽  
Tissue Samples ◽  
Whole Cells ◽  
Tissue Sections ◽  
Hepatic Cells ◽  
Slaughter House ◽  
Mammalian Tissues ◽  
Carbon Coated ◽  
Cellular Components

Crystalline intracellular inclusions are rarely seen in mammalian tissues and are often difficult to positively identify. Lymph node and liver tissue samples were obtained from two cows which had been rejected at the slaughter house due to the abnormal appearance of these organs in the animals. The samples were fixed in formaldehyde and some of the fixed material was embedded in paraffin. Examination of the paraffin sections with polarized light microscopy revealed the presence of numerous crystals in both hepatic and lymph tissue sections. Tissue sections were then deparaffinized in xylene, mounted, carbon coated, and examined in a Phillips 505T SEM equipped with a Tracor Northern X-ray Energy Dispersive Spectroscopy (EDS) system. Crystals were obscured by cellular components and membranes so that EDS spectra were only obtainable from whole cells. Tissue samples which had been fixed but not paraffin-embedded were dehydrated, embedded in Spurrs plastic, and sectioned.

Ultrastructural aspects of olfactory signal transduction and its development

1994 ◽  
Vol 52 ◽  
pp. 142-143
Author(s):  
Bert Ph. M. Menco
Keyword(s):  
Signal Transduction ◽  
Olfactory Receptor ◽  
Receptor Cell ◽  
Freeze Substitution ◽  
Luminal Surface ◽  
Tissue Sections ◽  
Olfactory Receptor Cells ◽  
Receptor Cells ◽  
Olfactory Signal ◽  
Odor Molecule

Vertebrate olfactory receptor cells are specialized neurons that have numerous long tapering cilia. The distal parts of these cilia line the interface between the external odorous environment and the luminal surface of the olfactory epithelium. The length and number of these cilia results in a large surface area that presumably increases the chance that an odor molecule will meet a receptor cell. Advanced methods of cryoprepration and immuno-gold labeling were particularly useful to preserve the delicate ultrastructural and immunocytochemical features of olfactory cilia required for localization of molecules involved in olfactory signal-transduction. We subjected olfactory tissues to freeze-substitution in acetone (unfixed tissues) or methanol (fixed tissues) followed by low temperature embedding in Lowicryl K11M for that purpose. Tissue sections were immunoreacted with several antibodies against proteins that are presumably important in olfactory signal-transduction.

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