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PubMed1980

Electron-probe x-ray analysis of granules and particles found in aurosomes produced by colloidal gold.

Aurosomes produced in the rabbit synovial membrane after intraarticular injection of colloidal gold were found to contain large spherical electron-dense granules and fine electron-dense particles. Electron-probe x-ray analysis demonstrated the presence of gold in the granules and iron in the particles. Sulphur and phosphorus were not detected in these aurosomes produced by colloidal gold. This is in contrast to the aurosomes produced by the soluble gold salt sodium aurothiomalate where besides gold, sulphur and phosphorus are easily detected.

Animals↗
PubMed1998

Nickel and gold in skin lesions of pierced earlobes with contact dermatitis. A study using scanning electron microscopy and x-ray microanalysis.

Cases of contact dermatitis due to nickel and gold especially in pierced earlobes, are increasing in number the world over. However, the presence of these metal fragments has not been demonstrated in the skin lesions. The aim of this study was to demonstrate nickel and gold in contact dermatitis lesions in pierced earlobes. Skin specimens taken from such earlobe lesions were examined using scanning electron microscopy and x-ray microanalysis. The pierced earrings worn when the lesions appeared were examined by the same techniques, and their analysis confirmed. In nickel dermatitis, small, electron-dense fragments were seen in the specimens examined by scanning electron microscopy, and nickel was detected in locations corresponding to these fragments by x-ray microanalysis. In contact dermatitis due to gold, small dense fragments containing gold were observed. It is suggested that small fragments of nickel and gold remain in the skin lesions of pierced earlobes for a long time, even after the studs have been removed, and cause prolonged irritation and various cutaneous reactions.

Adult↗
PubMed1988

Preparation of colloidal gold for staining proteins electrotransferred onto nitrocellulose membranes.

This paper describes a simple method of preparing colloidal gold for staining protein blots. Colloidal gold was prepared from 0.005 or 0.01% HAuCl4 by the addition of formalin as a reductant and potassium hydroxide. Staining of small cell carcinoma tissue extract blotted onto nitrocellulose membranes with this colloidal gold solution resulted in the appearance of a large number of clear wine-red bands. The sensitivity of gold staining was 60 times higher than that of Coomassie brilliant blue staining and almost comparable to that of silver staining of proteins in polyacrylamide gel. The sensitivity of this method was also satisfactory in comparison with that of enzyme immunoblotting. The colloidal gold prepared by this method is usable for routine work.

Blotting, Western↗
PubMed1989

The use of gold reagents to quantitate antibodies eluted from nitrocellulose blots: application to electron microscopic immunocytochemistry.

An assay is described in which gold reagents were used to quantitate nanogram amounts of antibody that had been eluted from antigens immobilized on nitrocellulose paper. Standard curves were generated by the application of rabbit immunoglobulin G (IgG) to nitrocellulose sheets assembled in a dot blot matrix apparatus. Blots were stained using either colloidal gold or immunogold, enabling quantitation of IgG concentration by scanning densitometry. Linear and reproducible standard curves were obtained. As little as 1 ng IgG/dot could be quantified using either gold reagent. In contrast to colloidal gold, immunogold could be used specifically to quantitate rabbit IgG regardless of the presence of bovine serum albumin or antigen coeluted from the nitrocellulose blot. The applicability of the immunogold assay was demonstrated by fractionating a complex rabbit antiserum raised against the RIM protein of frog retinal rod outer segments. Anti-RIM antibody was affinity-purified, quantitated by the immunogold assay, and subsequently employed in immunocytochemical studies using thin sections of retina embedded in a hydrophilic plastic, LR-Gold.

Animals↗
PubMed1984

Ultrastructural localization of gold in macrophages and mast cells exposed to aurothioglucose.

The ultrastructural localization of gold in resting, stimulated, and activated mouse peritoneal cells exposed in vivo and in vitro to aurothioglucose was examined by a photochemical technique. Activated macrophages from herpes simplex virus type 2 infected mice showed the heaviest accumulation of gold, located in phagolysosomes. Gold was also visualized in granules of mast cells and in nuclei of disintegrated cells. No gold was found in polymorphonuclear leucocytes and in lymphocytes. The mechanism by which gold is taken up into the cells is discussed.

Animals↗
PubMed1979

A quantitative and subjective characterization of tarnishing in low-gold alloys.

1. The quantitative objective characterization of tarnish gave results which are identical with those obtained from a blind subjective analysis. 2. The low-gold alloys fall into three classes. The alloy Ney Cast III is superior in performance to the other low golds and approximately equivalent to the high-gold alloy Firmilay. The intermediate alloys, including Midacast, Stabilor G, Mowrey No. 46, Tiffany, and Midas are similar in performance to the high-gold alloy Rx O.R.Y. The low-gold alloys Dent Cast 44, Minigold, and Progold tarnish in a manner which, in our opinion, makes them unacceptable.

Dental Alloys↗
PubMed1987

Effect of electrodeposition of gold on porcelain-to-metal bond strength.

The effect of electrodeposition of two different thicknesses of gold on porcelain-metal bond strength with three different base metal alloys was determined and compared to a control high gold alloy. The following conclusions can be drawn. Mean porcelain-metal bond strengths of all four alloys were in the same range when conventional porcelain application techniques were used. However, the base metal porcelain-metal bond is clinically suspect because of adhesive failure through the porcelain-metal interface. A thin 180A gold coat increased the porcelain-metal bond strength and generally resulted in cohesive failure through the porcelain. A thicker gold coat (720A) decreased the bond strength and generally resulted in adhesive failure. The mechanism of action of the gold coat on bond strength is likely its effect on the oxide layer on the surface of the base metal alloy.

Chemical Phenomena↗
PubMed1986

Mercury, silver, and gold inhibition of selenium-accelerated cysteine oxidation.

In vivo, cysteine in proteins or glutathione is the major amino acid involved in sulfhydryl oxidation-reduction reactions. An in vitro model of cysteine oxidation accelerated by selenium compounds was used to study the interaction of selenocystine and sodium selenite with metal ions. The interaction of metal ions with selenium compounds inhibited cysteine oxidation. The ionic forms of three toxic soft-acid metals, mercury, silver, and gold, were the most effective inhibitors. The antiarthritic gold drugs, aurothiomalate and aurothioglucose, were of particular interest as they inhibit the activity of selenium-glutathione peroxidase. The effect of gold ligands on gold(I) inhibition of selenocystine-accelerated cysteine oxidation was tested. Sodium cyanide partially reversed inhibition and potassium iodide had no effect. Inhibition of selenium-accelerated oxidation-reduction reactions by soft-acid metal ions may be of biological relevance during toxicities or during antiarthritic gold therapy.

Cysteine↗
PubMed1994

Combined intracellular injection of Neurobiotin and pre-embedding immunocytochemistry using silver-intensified gold probes in myenteric neurons.

We have developed methods to examine the neurochemistry of synaptic inputs to individual myenteric neurons labeled by dye injection through intracellular recording electrodes. Myenteric neurons of the guinea-pig ileum were filled with Neurobiotin, fixed, washed in 50% ethanol, exposed to sodium cyanoborohydride, incubated in avidin-biotin-horseradish peroxidase and incubated in antisera to calretinin or calbindin. The Neurobiotin-filled cells were revealed using the diaminobenzidine (DAB) reaction. The tissue was examined at the light microscope level to determine the morphology and projections of the Neurobiotin-filled neurons, and then incubated in 1 nm gold-labeled secondary antibodies. Following osmication, the gold probes were silver-intensified and the tissue embedded flat in resin. The tissue was re-examined at the light microscope level. Neurons containing a DAB reaction product could be distinguished from neurons containing a silver-intensified gold reaction product using oblique or epipolarized illumination. Ultrathin sections were taken through the injected neurons and examined. At the ultrastructural level, Neurobiotin-filled cell bodies and their processes (labeled with DAB) were easily distinguished from the structures labeled by silver-intensified gold. Gold-labeled terminals of enteric interneurons made synapses and close contacts with Neurobiotin-filled nerve cell bodies and their processes. This technique is valuable for the neurochemical identification of synaptic inputs to morphologically and/or functionally characterized myenteric neurons and could be easily applied to other preparations, such as brain slices.

Animals↗
PubMed1988

The use of colloidal gold immunoelectron microscopy to diagnose varicella-zoster virus (VZV) infections by rapid discrimination between VZV, HSV-1 and HSV-2.

Colloidal gold immunoelectron microscopy was used to diagnose rapidly 53 cases clinically suspected of varicella-zoster virus (VZV) infection and one special case selected from another study on typical herpes simplex virus (HSV) infections. The viruses were identified and subsequently typed within 2.5 h by a direct labelling test for VZV, and within 3.5 h by an indirect labelling test with monoclonal antibodies against HSV type 1 and type 2. The protein A purified IgG fraction of human anti-VZV immunoglobulins was adsorbed to colloidal gold particles, and the specificity of the gold-labelled antibodies was tested with several human and animal herpesviruses. Viral envelopes did not crossreact in the direct labelling test. However, an indirect labelling procedure revealed that a small fraction of the anti-VZV antibodies crossreacted with the cores of herpes simplex virus and pseudorabies virus (Aujeszky disease virus). Virus-infected cellular material taken from typical herpetic lesions was used directly without virus propagation for virus typing. All cases (N = 54) were analyzed without knowing the clinical description of the results of cytopathologic examination (Tzanck smear) and viral culture. Forty-four cases were identified as VZV; however, 5 of the supposed VZV infections were proved to be HSV infections. Although the viral culture of the one HSV case was HSV- and VZV-negative, colloidal gold labelling identified the case as VZV infection. In 16 cases virus immunoglobulin complexes were detected by using gold-tagged antibodies against human immunoglobulins. Immunoglobulins on the viral envelopes did not interfere with virus typing by immunogold labelling.

Antibodies, Viral↗
PubMed1993

Hepatonecrosis resulting from parenteral gold therapy in pemphigus vulgaris.

A patient who had pemphigus vulgaris received therapy with gold thiomalate in addition to dexamethasone. Three weeks after the initiation of parenteral gold the patient developed acute hepatitis. Causes other than gold toxicity were ruled out, and the patient recovered completely after discontinuation of gold therapy. This is the first case of acute hepatonecrosis resulting from gold therapy of pemphigus to be reported in the dermatologic literature.

Chemical and Drug Induced Liver Injury↗
PubMed1996

A characterisation of dark-field imaging of colloidal gold labels in a scanning transmission X-ray microscope.

While X-ray microscopes provide images of biological specimens for which the contrast is mainly due to the difference in the absorption of carbon and oxygen when X-rays transmitted through the specimen are detected, signals other than absorption can also be used to form images. Using the Stony Brook scanning transmission X-ray microscope at the National Synchrotron Light Source, high-angle dark-field images have been formed of cells labelled with colloidal gold, with and without silver enhancement. The high density of the colloidal gold particles, or the silver particles seeded by the gold, leads to a large scattering signal, and the fact that the particle diameters are comparable to the width of the microscope point spread function results in good localisation of the label with high contrast. The dark-field images can have a greater signal to noise ratio than bright-field images acquired with the same incident X-ray dose. The theory of dark-and bright-field imaging is reviewed. Theoretical calculations of scattering from gold and silver particles are presented and good agreement is found between these and experimental dark-field images of 30 nm diameter gold particles. The signal to noise ratios of experimental bright-and dark-field images are measured and found to be in agreement with theory. Images are presented of cells labelled by immunolabelling and in situ hybridisation.

Fibroblasts↗
PubMed1986

Are some major in vivo effects of gold related to microenvironments of decreased selenium?

Gold interacts with selenium in vivo, and the normal distribution of selenium among tissues and subcellular compartments changes. Literature evidence shows that many of the effects of gold compounds on the polymorphonuclear neutrophil, macrophage, and lymphocyte cellular components of the immune system are similar to effects observed in these cellular components in selenium-deficient animals. Affected by these two metals are immune functions related to phagocytic cell migration, phagocytosis, microbial killing, lymphocyte mitogenesis/DNA synthesis, arachidonic acid metabolism/prostaglandin synthesis, and immunoglobulin production. The interaction of gold with selenium in vivo may be responsible for some of the multiparameter-based actions of gold compounds used in the treatment of inflammatory diseases such as rheumatoid arthritis. One mechanism by which gold exerts its clinical effects may be related to its interaction with selenium to produce, in specific microenvironments, decreased levels of this essential trace element.

Animals↗
PubMed1989

Mapping Z-DNA tracts in plasmid DNA using electron microscopy and gold-labeled antibodies.

Using alternating poly(dG-dC).poly(dG-dC) and electron microscopy (EM), a method has been developed for detecting regions of Z conformation in DNA preparations. The procedure was developed with poly(dG-dC).poly(dG-dC) which had been converted to the Z conformation with MnCl2 and mild heat treatment. Conditions were found for reaction of this DNA with polyclonal anti-Z antibodies from rabbit, and further reaction of this mixture with gold-labelled anti-rabbit antibodies from mouse. Spreading of these samples onto air-water interfaces and examination by EM revealed gold particles aligned along strands of poly(dG-dC).poly(dG-dC). The method was refined and simplified using monoclonal antibodies and tested with the 2.2-kb plasmid, pDHg16, carrying a single tract of alternating d(G-C)23. Treatment with MnCl2 and mild heat was not necessary, as the superhelicity of this molecule ensured that the d(G-C) tract was in the Z conformation. Conditions were found for successful conjugation of mouse monoclonal anti-Z antibodies with colloidal gold (G10), 10.7-nm average diameter. The conjugate was then reacted with superhelical pDHg16, stabilized in polyethylene glycol and cross-linked with glutaraldehyde. Examination by EM showed gold particles at one site on the negatively superhelical circular DNA molecule. When these molecules were linearized with PstI, gold particles were found to occur at an average position 35% +/- 3% from one end. This location agrees well with the known position of the center of the alternating d(G-C) tract with respect to the PstI restriction site (36.8%).

Antibodies, Bacterial↗
PubMed1992

Comparison of colloidal gold electrode fabrication methods: the preparation of a horseradish peroxidase enzyme electrode.

In order to prepare biosensing electrodes which respond to hydrogen peroxide, horseradish peroxidase has been adsorbed to colloidal gold sols and electrodes prepared by deposition of these enzyme-gold sols onto glassy carbon using three methods: evaporation, electrodeposition and electrolyte deposition. In the latter method the enzyme-gold sol is applied to the surface of a glassy carbon disk electrode followed by an equal volume of 2 mM CaCl2. The electrolyte causes the sol to precipitate on the electrode surface, producing an immobilized enzyme electrode. Satisfactory electrodes which gave an electrochemical response to hydrogen peroxide in the presence of the electron transfer mediator ferrocenecarboxylic acid were produced by all three methods. Evaporation of horseradish peroxidase-gold sols produced electrodes with the best reproducibility and the widest linear amperometric response range. These electrodes can also easily be stored in a dry state. Although not as good as evaporation, electrodeposition also produced satisfactory electrodes. Electro-deposition provides the added advantage that it lends itself to the preparation of multi-enzyme/multi-analyte electrodes by the adsorption of different enzymes to separate gold sols, followed by sequential electrodeposition onto discrete areas of a multichannel electrode.

Biosensing Techniques↗
PubMed1991

High precision immunoscanning electron microscopy using Fab fragments coupled to ultra-small colloidal gold.

Ultra-small colloidal gold (less than 1 nm), bound to Fab fragments provides the shortest practical specific marker system to date and can be used in concert with field emission scanning electron microscopes to precisely locate antigenic sites. An "in-lens" FE-SEM equipped with a highly sensitive single crystal YAG-detector for backscattered electrons, as well as the use of advanced specimen preparation techniques based on cryofixation, are among the indispensible prerequisites. A T-even type Escherichia coli bacteriophage, Tu II*-46, was chosen to study properties of the immunogold labeling system. Distinct regions on the tail fibers of this phage were labeled with Fab fragments derived from antibodies against the related phage Tu II*-6. The tail fibers are composed of pairs of homologous proteins, thus offering two identical antigenic sites at the same locus on the tail fibers. Fab fragments can be visualized in the SEM at high accelerating voltage (30 kV) without any additional marker. This permits comparison of the labeling characteristics of unmarked and colloidal gold-marked Fab fragments. Unmarked Fab fragments often bind by pairs (two singlet Fab fragments bound opposed to each other along the axis of the tail fiber). The labeling efficiency of unmarked Fab fragments was greater than that of ultra-small gold-labeled Fab fragments. Binding by pairs was not seen after labeling with ultra-small gold-Fab fragments. The conjugates used in this study exhibited one colloidal gold per Fab fragment.

Animals↗
PubMed2005

A comparison of different strategies for the construction of amperometric enzyme biosensors using gold nanoparticle-modified electrodes.

A comparison of the analytical performances of several enzyme biosensor designs, based on the use of different tailored gold nanoparticle-modified electrode surfaces, is discussed. Glucose oxidase (GOx) and the redox mediator tetrathiafulvalene were coimmobilized in all cases by crosslinking with glutaraldehyde. The biosensor designs tested were based on the use of (i) colloidal gold (Au(coll)) bound on cysteamine (Cyst) monolayers self-assembled on a gold disk electrode (AuE) and (ii) glassy carbon electrodes (GCEs) modified with electrodeposited gold nanoparticles (nAu). The results obtained with these designs were compared with those provided by a GOx/Cyst-AuE and a GOx/MPA-AuE. In the second case (ii), configurations based on direct immobilization of GOx on nAu (GOx/nAu-GCE) or on Cyst or MPA self-assembled monolayers (SAMs) previously bound on gold nanoparticles (GOx/Cyst-nAu-GCE or GOx/MPA-nAu-GCE, respectively) were compared. The analytical characteristics of glucose calibration plots and the kinetic parameters of the enzyme reaction were compared for all of the biosensors tested. The GOx/Au(coll)-Cyst-AuE design showed a sensitivity for glucose determination higher than that achieved with GOx/Cyst-AuE and GOx/Au(coll)-Cyst/Cyst-AuE and similar to that achieved with GOx/MPA-AuE. Moreover, the useful lifetime of one single GOx/Au(coll)-Cyst-AuE was 28 days, remarkably longer than that of the other GOx biosensor designs.

Biosensing Techniques↗
PubMed2004

Mitochondrial thioredoxin reductase inhibition by gold(I) compounds and concurrent stimulation of permeability transition and release of cytochrome c.

The effects of auranofin, chloro(triethylphosphine)gold(I) (TEPAu), and aurothiomalate on mitochondrial respiration, pyridine nucleotide redox state, membrane permeability properties, and redox enzymes activities were compared. The three gold(I) derivatives, in the submicromolar range, were extremely potent inhibitors of thioredoxin reductase and stimulators of the mitochondrial membrane permeability transition (MPT). Auranofin appeared as the most effective one. In the micromolar range, it inhibited respiratory chain and glutathione peroxidase activity only slightly if not at all. TEPAu and aurothiomalate exhibited effects similar to auranofin, although TEPAu showed a moderate inhibition on respiration. Aurothiomalate inhibited glutathione peroxidase at concentrations where auranofin and TEPAu were without effect. Under nonswelling conditions, the presence of auranofin and aurothiomalate did not alter the redox properties of the mitochondrial pyridine nucleotides indicating that membrane permeability transition occurred independently of the preliminary oxidation of pyridine nucleotides. Under the same experimental conditions, TEPAu showed a moderate stimulation of pyridine nucleotides oxidation. Mitochondrial total thiol groups, in the presence of the gold(I) derivatives, slightly decreased, indicating the occurrence of an oxidative trend. Concomitantly with MPT, gold(I) compounds determined the release of cytochrome c that, however, occurred also in the presence of cyclosporin A and, partially, of EGTA, indicating its independence of MPT. It is concluded that the specific inhibition of thioredoxin reductase by gold(I) compounds may be the determinant of MPT and the release of cytochrome c.

Animals↗