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PubMed1985

Effects of storage conditions on platelet cytoskeletal proteins.

The platelet cytoskeleton is a major determinant of platelet morphology and function. Changes in the protein composition of the cytoskeleton were studied during storage of platelets at 20 degrees to 24 degrees C under blood banking conditions. Cytoskeletons were prepared by extraction of washed platelets with the detergent Triton X-100 and then analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In addition to the three major proteins visible with Coomassie blue staining--actin, myosin, and actin-binding protein--silver staining revealed other proteins associated with the cytoskeletons of freshly collected and stored platelets. The resting platelet cytoskeleton contained 8% to 10% of the total platelet protein and approximately 50% of the total actin. During storage of platelet concentrates for up to five days in the PL 732 container, proteins of 50,000 to 55,000 and 90,000 mol wt were increasingly incorporated into the Triton-insoluble fraction, whereas the amounts of cytoskeleton-associated actin-binding protein, myosin, and actin were maintained at levels present in fresh platelets. Storage of platelets under conditions that allowed the reduction of platelet concentration pH to nearly 6.0 resulted in a marked decrease in the amounts of the major proteins of the cytoskeleton. The loss of specific proteins from platelets stored for extended periods with reduced pH, accompanied by the appearance of lower molecular weight proteins in the cytoskeleton, suggests that extensive proteolysis may occur under certain storage conditions. These data show that the conditions employed for storage of platelet concentrates influence the protein composition of the cytoskeleton and the total protein content of the platelet.

Blood Banks↗
PubMed1985

Corneal argyrosis: histologic, ultrastructural and microanalytic study.

The clinical, histopathological, ultrastructural and microanalytic features of a case of iatrogenic ocular argyrosis are reported. The case, in a 63-year-old woman with long-standing herpetic keratitis, was unusual in that it occurred after apparently only one treatment with eyedrops consisting of a 1% solution of "mild silver protein" (Argyrol). Another unusual feature was that the silver deposited in the cornea was mainly conjugated to sulfur; selenium, which commonly demonstrates a high affinity for silver in tissues, was detectable in only trace amounts.

Argyria↗
PubMed1991

On the relationship of amino acid composition to silver staining of proteins in electrophoresis gels: II. Peptide sequence analysis.

The quantification of proteins in silver-stained electrophoresis gels has been limited by the differences in "stainability" of different proteins. Despite efforts by many researchers, the precise basis of the reaction between silver reagents and polypeptides is still unclear, and, depending on the formulation, may even differ. We have tested the hypothesis that differences in stainability among proteins can be attributed to differences in di- or tripeptide composition. The results indicate that some order of protein structure other than short peptides accounts for the staining differences observed.

Amino Acid Sequence↗
PubMed1998

Effect of light on generation of colored silver colloids in protein solutions.

The exposure to light (20 mW/cm2, an incandescence lamp) of weakly alkaline protein solutions which contained silver nitrate and formaldehyde initiated reduction of silver ions with the subsequent generation of colored silver colloids. At light intensities lower than 0.2 mW/cm2 the generation of colored silver colloids was delayed. The rate of silver reduction depended on the protein type and on the light spectral structure. In particular, solutions which contained prealbumin, lysozyme, gamma-globulin, and transferrin were more photosensitive than solutions which contained albumin, pepsin, and beta-amylase. The formation of [Ag(NH3)2]+ complex after an addition of ammonium ions into the solutions preferentially suppressed silver reduction in the dark and under exposure to red light, thus resulting in a significant difference in the time of appearance of colored silver colloids when the solutions were exposed to violet or red light. These findings are promising for the elaboration of selective silver development of proteins in polyacrylamide gels.

Animals↗
PubMed1986

Requirement for cysteine in the color silver staining of proteins in polyacrylamide gels.

To determine whether cysteine residues have a contribution to the mechanism of color silver staining, we silver stained sodium dodecylsulfate polyacrylamide gel electrophoresis separations of proteins which have few or no cysteines. Proteins without cysteine stained negatively (yellow against a yellow background) with silver. Proteins with one or more cysteines stained orange, red, brown, or green/gray depending on the mole percentage of cysteine and whether they contained covalently attached lipids. The colors could not be correlated with the mole percentages of cysteine of these proteins indicating that some components other than cysteine affect the staining color of cysteine-containing proteins. Silver staining of amino acids, sugars, nucleotide bases, or lipopolysaccharide dot-blotted onto nitrocellulose paper implicated adenine, lipids, the basic amino acids, and glutamine, but not sugars or other amino acids in silver/protein complexes.

Bacterial Outer Membrane Proteins↗
PubMed1990

A method for histochemical demonstration of protein-bound amino groups by light microscopy.

We have established an efficient method for the histochemical demonstration of protein-bound amino groups by light microscopy, using a ninhydrin or alloxan-thiocarbohydrazide-silver proteinate (NHY or ALX-TCH-SP) sequence followed by a physical development (PD) procedure. As a result of the present experimental studies on Carnoy's solution-fixed paraffin sections of a series of rat tissues, including three types of major salivary glands, liver, pancreas, stomach, duodenum, jejunum, colon, kidney, prostate, and spleen, the sensitivity and specificity of the new method were found to be sufficient. In the tissues tested, protein-bound amino groups were visualized by distinct brownish or blackish reaction products. Comparisons of the particular method with the NHY or ALX-Schiff methods employed hitherto have substantiated the fact that the former method leads to apparently higher visibility of reaction products than the latter.

Alloxan↗
PubMed2001

The scaled volume as an image analysis variable for detecting changes in protein expression levels by silver stain.

A new variable for measuring the relative intensities of silver stained protein spots on two-dimensional gels is described. The scaled volume (SV) more accurately measures the intensity of protein spots and accounts for differences frequently encountered when trying to compare two gels than other variables such as relative volume ratio, optical density, or relative optical density. The SV scales the signal of interest by the noise (gel background) with secondary signals removed (spots not of interest, e.g., technical artifacts). The SV of spot intensities offers a better dynamic response to protein amount for the model proteins studied here. Depending on the quantity of protein loaded onto gels, we have observed a coefficient of variation range of 0.2 to 1.3. We also observe that the SV silver stain response follows a characteristic exponential profile for different proteins.

Animals↗
PubMed2000

Assessment of explanted PTCA balloons.

The data presented here are part of a on-going study to define the surface characteristics and properties of explanted PTCA catheters in a further effort to address some of the ramifications of the re-use issue. PTCA balloon catheter were examined after angioplasty in one hundred and sixty-eight patients (n = 168). This series included six balloon types from three manufacturers. The fresh fixed and dehydrated balloons were examined at first with light microscopy and then in a scanning electron microscope. X-ray semiquantitative microanalysis and FT-IR-ATR analysis were also performed on the balloons. Because most blood proteins are water soluble, we examined unfixed balloons with a protein silver staining kit for detection of adhered proteins described by Heukeshoven. A further method for protein detection is the Lowry-analysis. With this method water insoluble proteins can be observed. Our study has shown convincingly that all deployed angioplasty catheters were coated with adherent protein layers. Plaque particles were found embedded in the surfaces of most of the balloons examined. Fissuring and micro tearing of balloon surfaces was noted. FT-IR-ATR analyses of the blood contacted balloon surfaces did not show any peaks indicative of proteins on the balloon surface. The silver staining method also did not show any evidence of protein adsorption on the balloons. On the other hand, the Lowry-analysis yielded clear evidence that water insoluble proteins were adherent to the balloon surfaces. The average measured protein concentration was 17 microg/ml.

Angioplasty, Balloon, Coronary↗
PubMed1987

Argyrosis of the lacrimal sac.

Silver deposition in the wall of the lacrimal sac after prolonged application of mild silver protein (Argyrol) eye drops is documented at the light and electron microscopical level. Silver granules were found in the extracellular matrix predominantly on elastic fibres and within cells forming conglomerates in secondary lysosomes. Most of the silver-containing cells showed a prominent rough endoplasmic reticulum, suggesting their fibroblastic origin. Investigation by energy-dispersive analysis of X-rays (EDAX) indicated the precipitation of silver as selenide.

Aged↗
PubMed1983

Identification of a yellow gene-specific protein in Drosophila melanogaster by two-dimensional gel electrophoresis.

Analysis of temperature-sensitive mutants suggests that the yellow (y) gene in Drosophila melanogaster is expressed at a different time in each cell type that gives rise to the various structures of the adult cuticle. An important step in analyzing the regulation of this gene requires identification of the y structural protein. A polypeptide has been identified which correlates with the presence or absence of a functional y gene. Furthermore, this protein has the tissue distribution profile expected of the y structural gene product. The ability to locate this gene was facilitated by the use of coisogenic stocks, two-dimensional electrophoretic protein separation, and an ultrasensitive silver protein stain.

Animals↗
PubMed1983

New aspects on the 'rodlet cell' in teleosts.

The enigmatic rodlet cells, hitherto interpreted mainly as unidentified parasitic stages ('Rhabdospora thélohani') or as a sort of secretory cell, have been studied with electron microscopical and histochemical methods in three teleost species (Cyprinus carpio L., Tinca tinca L., Salmo gairdneri Rich.). The typical inclusions, the rodlets, consist of a dense core and a less dense cortex, with a coarse flocculent outer zone. The latter shows a positive reaction for neutral polysaccharides respectively glycoproteins (with the silver proteinate method and the equivalent silver methenamine-staining), concurring with some of the light microscopic data. While this suggests the secretion of this material by the Golgi apparatus, the core gives contradictory results, pointing to genetic material instead of a secretory product. Although the Feulgen method (as standard test for DNA with only a few exceptions known) is negative, DNA is indicated by several other methods (light microscopical fluorescence staining with HOECHST 33258, EDTA-method after Bernhard (1969), enzyme digestions positive with DNAse and negative with RNAse). Taken together with some observations on the tissue reaction (phagocytosis of the often discharged rodlets by macrophages and also the more specifically acting heterophilic granulocytes; isolation of the rodlet cells from the adjoining tissue as seen e.g. with the ruthenium red method), an exogenous parasitic nature of these cells seems more plausible, even if the evidence is not sufficient for an exact classification of either the cell or its characteristical inclusions.

Animals↗
PubMed1996

Silver products for medical indications: risk-benefit assessment.

BACKGROUND: Legitimate medicinal use of silver-containing products has dramatically diminished over the last several decades. Recently, however, some manufacturers have begun to enthusiastically promote oral colloidal silver proteins as mineral supplements and for prevention and treatment of many diseases. Indiscriminate use of silver products can lead to toxicity such as argyria. OBJECTIVE: To assist health care professionals in a risk versus benefit assessment of over-the-counter silver-containing products, we herein examine the following issues: historical uses, chemistry, pharmacology, clinical toxicology, case reports of adverse events in the literature, and the recent promotion of over-the-counter silver products. Other sources of silver exposure (including environmental and dietary) and EPA exposure standards are discussed. A list of currently available silver products is provided for easy reference and screening. CONCLUSIONS: We emphasize the lack of established effectiveness and potential toxicity of these products.

Animals↗
PubMed1995

Anti-inflammatory properties of copper, gold and silver, individually and as mixtures.

It has been previously demonstrated that the mixture of Cu, Au and Ag impaired significantly the clinical and biochemical disorders induced by adjuvant arthritis in the rat. The efficiency of this mixture and of each component was tested on the same animal model. Treated rats were injected daily with either 22.8 micrograms of copper gluconate, 0.2 micrograms of gold thioglucose, 6.8 micrograms of silver proteinate or the blended solution over a period of 29 d. The treatment with the one component solutions was found to have a little or no effect on the plasma levels of fibrinogen, haptoglobin, ceruloplasmin, prostaglandin E2, thromboxane B2, total proteins, Zn, Cu, Mn, Se, Co and Ni, and no significant decrease was observed in the paw oedema resulting from the Freund's adjuvant injection. The treatment with the mixture had a significant preventive effect. Therefore it seems that the administration of low doses of each of the three trace elements have no anti-rheumatic property in the rat. The results indicate an enhanced effect of the metal mixture in the model studied.

Animals↗
PubMed1982

[Silver stain of unconcentrated cerebrospinal fluid. Preliminary results in multiple sclerosis and other neurological diseases].

The authors present a new technique for the analysis of the cerebro spinal fluid (C.S.F.) proteins: silver stain after isoelectric focusing with possibility of immunofixation. This technique is simple and results are obtained after six hours only after sample deposition. If immunofixation is used a further 24 hours washing is necessary. It is highly sensitive and bands containing 25 ng of proteins can be clearly distinguished so that small volumes (10 microl. at mean) of unconcentrated C.S.F. can be used. With this technique abnormal distinct bands of IgG specificity are seen in the majority of central and peripheral nervous system inflammatory disorders. No distribution of these bands, particularly in the more cathodal zone, seems to be specific of any disease including multiple sclerosis (M.S.). The abnormal IgG bands in M.S.C.S.F. seem to have their counterpart in the serum. These results need further verification. The usefulness of this technique for research purposes is stressed. The protein pattern obtained must be interpreted in the light of the concepts of genetic polymorphism, microheterogeneity and heterogeneous mode of antibody production.

Cerebrospinal Fluid Proteins↗
PubMed1988

Ultrastructural silver enhancement of Prussian blue-reactive iron in hematopoietic and intestinal cells.

Prussian blue has been widely used to localize iron in a variety of tissues at the light and electron microscopic level. In the present study, thin sections of human marrow and blood cells and rat duodenal cells were exposed to silver proteinate (SP) after staining en bloc with acid ferrocyanide (AF), with and without prior iron saturation using iron nitrilotriacetate (FeNTA). Silver deposition was observed over Prussian blue-reactive sites and significantly enhanced sites of minimal AF and FeNTA-AF staining. AF-SP stain deposits were present in the cytoplasmic matrix, granules, and occasionally on the surfaces of macrophages, monocytes, and erythroblasts. FeNTA-AF-SP stained additional cytoplasmic and surface sites in erythroblasts and stained neutrophil granules intensely. Duodenal epithelium from iron-loaded rats demonstrated strong AF-SP staining of ferric iron in microvilli, apical cytoplasmic matrix, and lateral membranes. Similar preparations from iron-replete rats stained sparsely; however, intense AF-SP staining was observed after iron saturation with FeNTA. SP similarly enhanced luminal ferrous iron deposits stained with acid ferricyanide in rats given intraluminal ferrous iron. AF-SP stain deposits were removed by exposure of thin sections to NH4OH, KCN, or HNO3 but were not affected by prior exposure to HIO4 or NaBH4, consistent with a silver cyanide or complex stain precipitate rather than reduced silver or silver ferriferrocyanide. SP enhancement of Prussian blue allows identification of reactive sites not readily visualized with AF or FeNTA-AF alone, and offers the potential for differentiating AF staining from other deposits or organelles of comparable density.

Animals↗
PubMed1987

Tryptic peptide analysis of nanogram quantities of proteins: radioiodination of proteins detected by silver staining in polyacrylamide gels.

The silver-staining procedure for detecting proteins in polyacrylamide gels has been modified so that the polypeptides remain suitable for subsequent radioiodination and tryptic peptide analysis. The procedure, which involves a silver-staining/destaining protocol that minimizes crosslinking, is more rapid than many other methods, and can detect as little as 1 ng of protein. Following elimination of silver, the proteins can be radioiodinated and digested with trypsin by a modification of the method described by J. H. Elder, R. A. Pickett, J. Hampton, and R. A. Lerner (1977, J. Biol. Chem. 252, 6510-6515). Together, these improvements have increased the sensitivity of the tryptic peptide mapping technique by three orders of magnitude and thereby enabled us to perform reproducible structural analysis of femtomolar quantities of proteins.

Electrophoresis, Polyacrylamide Gel↗
PubMed1986

Modified method of silver staining of proteins in polyacrylamide gels.

The very sensitive and reliable silver staining method to visualize proteins in polyacrylamide gels described by Wray et al. (Anal. Biochem. (1981) 118, 197-203) fails when the protein sample contains nucleic acids and/or metals. By washing the polyacrylamide gels in acetic acid and repeatedly in methanol immediately following electrophoresis and then using the procedure of Wray et al., many gels otherwise unstainable may be stained with a high degree of reliability. This method allows visualization of a minute amount of proteins in samples containing high amounts of DNA and metals.

Cell Line↗
PubMed1987

Improved Thiéry staining for the ultrastructural detection of polysaccharides.

The use of silver vitellinate instead of silver proteinate in the Thiéry's staining for the ultrastructural detection of polysaccharides has advantages which derive from the lesser reactivity and higher stability of silver vitellinate solutions, allowing the obtention of a finer staining of periodic acid-Schiff (PAS)-positive materials with a cleaner background. The proposed method is particularly useful for the staining of PAS-positive cellular components at high resolution.

Animals↗