scholarly journals Ultrastructural localization of carbohydrates on thin sections of Staphylococcus aureus with silver methenamine and wheat germ agglutinin-gold complex.

1987 ◽  
Vol 169 (3) ◽  
pp. 1358-1362 ◽  
Author(s):  
H Morioka ◽  
M Tachibana ◽  
A Suganuma
Keyword(s):  
Staphylococcus Aureus ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Ultrastructural Localization ◽  
Gold Complex ◽  
Thin Sections

scholarly journals Ultrastructural localization of concanavalin A and wheat germ agglutinin binding sites in adult and embryonic mouse myocardium.

1982 ◽  
Vol 30 (3) ◽  
pp. 193-200 ◽  
Author(s):  
D Gros ◽  
B Bruce ◽  
C E Challice ◽  
J Schrevel
Keyword(s):  
Concanavalin A ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Ultrastructural Localization ◽  
Embryonic Cells ◽  
Con A ◽  
Embryonic Mouse ◽  
Transverse Tubular System ◽  
Receptor Sites ◽  
Ultrathin Sections

The lectins, concanavalin A (Con A) and wheat germ agglutinin (WGA), have been used to localize with precision glycosyl residues in adult and embryonic mouse myocardium. They were detected by means of an affinity method using peroxidase and chitobiosylperoxidase, respectively, which then were revealed with 3,3'-diaminobenzidine and H2O2. Exhaustive controls have shown that the binding of Con A and WGA is reversible when experiments are performed with adult specimens (tissue blocks or ultrathin sections of glycol methacrylate-embedded material) or with isolated embryonic cells. Experiments carried out with tissue blocks from embryonic hearts have shown peroxidase binding. This finding is discussed on the basis of the presence of the endogenous lectin-like components in embryonic hearts. Results show that the surface of adult and embryonic myocardial cells specifically bind both Con A and WGA, thus indicating the presence of glycosyl residues similar to alpha-methyl-D-mannoside and N-acetyl-D-glucosamine. In adult heart the transverse tubular system was also labeled. The absence of Con A and WGA receptor sites in the gap junction regions was demonstrated by means of an electron microscope postembedding staining method.

scholarly journals Ultrastructural localization of nuclei acids by the use of enzyme-gold complexes.

1981 ◽  
Vol 29 (4) ◽  
pp. 531-541 ◽  
Author(s):  
M Bendayan
Keyword(s):  
Secretory Granules ◽  
Ultrastructural Localization ◽  
Rnase A ◽  
Gold Complex ◽  
Gold Complexes ◽  
Thin Sections ◽  
Gold Particles ◽  
Enzyme Substrate ◽  
Cellular Compartments ◽  
Cytochemical Technique

A cytochemical technique for the ultrastructural localization of substrates using enzyme-gold complexes is reported. RNase A and DNase I have been labeled with gold particles. The RNase-gold and dNase-gold complexes obtained were applied on thin sections of glutaraldehyde-fixed and Epon-embedded tissues. Different cellular compartments were labeled by these enzyme-gold complexes. Using the RNase-gold complex the rough endoplasmic reticulum appeared decorated with gold particles. The gold marker was also present over the nucleus, especially over the nucleolus; mitochondria were weakly labeled. Using the DNase-gold complex, gold particles were concentrated over the euchromatin of the nucleus and the mitochondria. The heterochromatin and the nucleolus showed a less intense labeling. For both enzyme-gold complexes, the Golgi area, the secretory granules and the extracellular space appeared free of label. In those control conditions where the substrates were added to the enzyme-gold complexes a major reduction in the labeling was observed. A quantitative evaluation of the labeling was performed. This evaluation confirmed the qualitative observations and the marked reduction of labeling occurring under the control conditions. The combination of the specificity of the enzyme-substrate interactions with the size and electron density of the gold particles and the good ultrastructural preservation of the tissues resulted in a very specific labeling with high resolution. These results demonstrate the possibility of detecting substrates by means of enzyme-gold complexes at the electron microscope level.

scholarly journals Staining of serous acinar cells of human parotid gland with wheat germ agglutinin-gold complex.

1985 ◽  
Vol 18 (4) ◽  
pp. 391-394 ◽  
Author(s):  
MITSUO MACHINO ◽  
HIROYUKI MORIOKA ◽  
MASAYOSHI TACHIBANA
Keyword(s):  
Parotid Gland ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Acinar Cells ◽  
Gold Complex ◽  
Human Parotid Gland

scholarly journals Ultrastructural localization of intracellular antigens by the use of protein A-gold complex.

1978 ◽  
Vol 26 (12) ◽  
pp. 1074-1081 ◽  
Author(s):  
J Roth ◽  
M Bendayan ◽  
L Orci
Keyword(s):  
Endocrine Pancreas ◽  
Protein A ◽  
Ultrastructural Localization ◽  
Gold Complex ◽  
Secretory Proteins ◽  
Staphylococcal Protein A ◽  
Thin Sections ◽  
Antigenic Sites ◽  
Step Procedure ◽  
General Method

An immunocytochemical technique for the demonstration of intracellular antigens (secretory proteins) on thin sections is reported. Staphylococcal protein A which reacts with the Fc fragment of IgG molecules was labeled with colloidal gold as a marker. The antigenic sites were visualized on aldehyde-fixed and Epon-embedded tissue in a two step procedure. The specific antisera were applied to thin sections for binding to the antigens and then visualized by the protein A-gold complex. By using this technique different secretory proteins of the exocrine and endocrine pancreas were localized. The protein A-gold technique is proposed as a general method for visualization of antigenic sites on thin sections.

scholarly journals Localization of sugar-binding sites in Staphylococcus aureus using gold-labeled neoglycoprotein.

1994 ◽  
Vol 42 (12) ◽  
pp. 1609-1613 ◽  
Author(s):  
H Morioka ◽  
A Suganuma ◽  
M Tachibana
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Bovine Serum Albumin ◽  
Binding Sites ◽  
Bacterial Strain ◽  
Wheat Germ ◽  
Electron Microscopic ◽  
Thin Sections ◽  
Gold Particles ◽  
Sugar Binding

We studied post- and pre-embedding staining of sugar-binding sites on thin sections of Staphylococcus aureus with an electron microscopic neoglycoprotein-gold technique. Although gold particles of cellobiosyl bovine serum albumin (BSA)-glycosylated BSA-, lactosyl BSA-, and melibiosyl BSA-gold did not label, heavy labeling of N-acetylglucosaminide-BSA-gold was observed in both the cell wall and the cytoplasm on Spurr-embedded thin sections of S. aureus. Inhibition of labeling with wheat germ agglutinin-biotin and N-acetylglucosaminidase indicated that the labeling was due to N-acetylglucosamine. These data suggested that molecules that bind specifically with N-acetylglucosamine occur in the cell wall and cytoplasm of S. aureus. Pre-embedding staining revealed that these molecules are abundant at the surface of the cell wall and that the abundance differs depending on the bacterial strain. An N-acetylglucosamine-specific lectin-like substance, glucosaminidase, and toxins are proposed as candidates for molecules responsible for the labeling, and the possible functional significance of the findings is discussed briefly.

Ultrastructural Localization of Phycocyanin in the Acidophilic, Thermophilic Alga, Cyanidium Caldarium

1973 ◽  
Vol 31 ◽  
pp. 462-463
Author(s):  
M. R. Edwards ◽  
J. D. Mainwaring
Keyword(s):  
Yellowstone National Park ◽  
National Park ◽  
Ultrastructural Localization ◽  
Review Of Literature ◽  
Cyanidium Caldarium ◽  
Taxonomic Rank ◽  
Thin Sections ◽  
Standard Methods ◽  
Laboratory Cultures

Although the general ultrastructure of Cyanidium caldarium, an acidophilic, thermophilic alga of questionable taxonomic rank, has been extensively studied (see review of literature in reference 1), some peculiar ultrastructural features of the chloroplast of this alga have not been noted by other investigators.Cells were collected and prepared for thin sections at the Yellowstone National Park and were also grown in laboratory cultures (45-52°C; pH 2-5). Fixation (glutaraldehyde-osmium), dehydration (ethanol), and embedding (Epon 812) were accomplished by standard methods. Replicas of frozenfracture d- etched cells were obtained in a Balzers apparatus. In addition, cells were examined after disruption in a French Press.

Immunogold localization of HMB-45 antigen in pulmonary lymphangiomyomatosis

1995 ◽  
Vol 53 ◽  
pp. 998-999
Author(s):  
J.M. Minda ◽  
E. Dessy ◽  
G. G. Pietra
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Room Temperature ◽  
Osmium Tetroxide ◽  
Muscle Cells ◽  
Ultrastructural Localization ◽  
Reproductive Age ◽  
Thin Sections ◽  
Smooth Muscle Proliferation ◽  
Hmb 45

Pulmonary lymphangiomyomatosis (PLAM) is a rare disease occurring exclusively in women of reproductive age. It involves the lungs, lymph nodes and lymphatic ducts. In the lungs, it is characterized by the proliferation of smooth muscle cells around lymphatics in the bronchovascular bundles, lobular septa and pleura The nature of smooth muscle proliferation in PLAM is still unclear. Recently, reactivity of the smooth muscle cells for HMB-45, a melanoma-related antigen has been reported by immunohistochemistry. The purpose of this study was the ultrastructural localization of HMB-45 immunoreactivity in these cells using gold-labeled antibodies.Lung tissue from three cases of PLAM, referred to our Institution for lung transplantation, was embedded in either Poly/Bed 812 post-fixed in 1% osmium tetroxide, or in LR White, without osmication. For the immunogold technique, thin sections were placed on Nickel grids and incubated with affinity purified, monoclonal anti-melanoma antibody HMB-45 (1:1) (Enzo Diag. Co) overnight at 4°C. After extensive washing with PBS, grids were treated with Goat-anti-mouse-IgG-Gold (5nm) (1:10) (Amersham Life Sci) for 1 hour, at room temperature.

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