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Query: KEGG:D04166 (FeCl3)
 1,389 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Since Pearse in 1957 introduced chromoxane cyanine R as a dual nuclear and cytoplasmic stain there have appeared numerous procedures for use of this dye. These have differed widely, sharing in common mainly the implication that each is best. A defendable procedure has been developed on an experimental basis and is reported here. Four stock solutions are needed: (1) a 0.2% solution of chromoxane cyanine R in 0.5% aqueous H2SO4 (v/v); boil this solution for 5 min, (2) 10% FeCl3 in 3% HCl, (3) 1% aqueous HN4OH, and (4) 1% HCl in 70% ethanol. The staining solution: 40 ml of dye solution, 2 ml of FeCl3 solution, 8 ml H2O. Dewax and hydrate sections and stain for 10 min. If a myelin sheath stain is desired differentiate for 1 min in solution (3). For a nuclear stain differentiate for 1 min in solution (4). The nuclear stain when counterstained with eosin closely resembles the routine hematoxylin and eosin. Histochemical tests show that the functional group for myelin staining contains nitrogen, and probably hydrogen bonding is involved. The nuclear stain involves a different functional group and possibly neither electrostatic nor hydrogen bonding.
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PMID:Staining with chromoxane cyanine R. 9 54

A membrane filter procedure has been developed for the rapid quantitation of C. perfringens in the aquatic environment. Background growth is inhibited by the use of D-cycloserine, polymyxin B sulfate, and incubation at 45 degrees C. Differential characteristics include the fermentation of sucrose, production of acid phosphatase, and the absence of beta-D-glucosidase activity. The medium is prepared as follows (in grams per 100 ml of distilled water): tryptose, 3.0; yeast extract, 2.0; sucrose, 0.5; L-cysteine, 0.1; MgSO4. 7H2O, 0.01; bromocresol purple, 0.004; and agar, 1.5. The ingredients are dissolved, and the pH is adjusted to 7.6. After autoclaving at 121 degrees C for 15 min, the medium is allowed to cool at 50 degrees C, and the following are added per 100 ml: D-cycloserine, 40 mg; polymyxin B sulfate, 2.5 mg; indoxyl-beta-D-glucoside, 60 mg; 2.0 ml of a filter-sterilized 0.5% phenolpthalein diphosphate solution; and 0.2 ml of a filter-sterilized 4.5% FeCl3.6H2O solution. Enumeration of C. perfringens in a water sample is completed within 18 to 24 h. The verification of typical colonies was 93%. The average recovery from peptone-water spore suspensions of five strains was 79%, and that from filter-sterilized seawater suspensions was 90%. The precision of the method was approximately equal to that expected from random error alone. Confirmed recoveries of C. perfringens from water and sewage samples generally were greater than those by the Bonde pour tube method.
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PMID:Membrane filter enumeration method for Clostridium perfringens. 21 10

Three groups of methods for analyzing nitrite in meat are compared. All methods consist of a sequence of steps, grouped according to initial extraction procedures. In Group 1, the sample is treated with borate followed by HgCl2 or Carrez I, and then Carrez II. In Group 2, the sample is diluted with water, heated at 80 degrees C, and analyzed immediately (AOAC) or after addition of either Na2CO3 and FeCl3 or HgCl2. In Group 3, the sample is made alkaline with NH4Cl buffer and then treated with one of the following: activated carbon plus Carrez I and II, alumina cream, or AIK(SO4)2. At each step when the method involved the addition of a chemical, supernates and precipitates (if formed) were analyzed for nitrite by Griess reagent both before and after AOAC digestion. The normally discarded precipitates formed after addition of HgCl2 and Carrez I and II contained bound nitrite that could be detected by AOAC analysis. Except in the AOAC method, HgCl2 improved nitrite analysis. Results by AOAC analysis were 3 to 300% higher than those determined after addition of any chemical or combination of chemicals. Spiked meat samples could not be used in comparing nitrite analysis methods because results were misleading. Acid meat samples, such as fermented sausages, required neutralization before AOAC analysis.
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PMID:Comparison of sample preparation procedures for colorimetric analysis of nitrite in frankfurters. 72 22

A taste cell mucosal surface is regarded as a planar region containing bound anionic sites and openings to ionic channels. It is assumed that the bulk aqueous properties of the exterior phase are not continuous with the surface but terminate at a plane near the surface. The region between the (Stern) plane and the membrane is regarded as having a lower dielectric constant than bulk water. This fact admits the possibility of ion pair formation between fixed sites and mobile cations. Mobile ion pairs entering the region may also bind to a fixed anionic site. Thus, it is assumed that mobile cations and ion pairs are potential determining species at the surface. Binding cations neutralizes surface charges, whereas binding mobile ion pairs does not. This competition accounts for the observed anion effect on stimulation of tast receptors by sodium salts. The potential profile is constructed by superimposing the phase boundary potentials with an ionic diffusion potential across the membrane. The model accounts for the anion effect on receptor potential, pH effects, the reversal of polarity when cells are treated with FeCl3, and the so-called "water reponse," depolarization of the taste cell upon dilution of the stimulant solution below a critical lower limit. The proposed model does not require both bound cationic and anionic receptors, and further suggests that limited access to a Stern-like region continuous with membrane channels may generally serve to control transport of ions.
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PMID:A model for the stimulation of taste receptor cells by salt. 93 27

ATP-Fe and AMP-Fe complexes in water (H2O and 2H2O) at pH 7.5 were studied using Raman spectroscopy. Parallel and perpendicular polarization spectra were recorded in the spectral range 200-1650 cm-1, and the depolarization ratios for most of the bands were calculated. The changes in the frequencies, intensities and depolarization ratios of the ATP and AMP bands after the addition of FeCl3 showed that the adenine moiety, in addition to the phosphate(s), was involved in the binding of Fe to both ATP and AMP. Direct interactions of Fe(III) with the phosphate chain and the N-7 nitrogen and indirect interaction (via water molecules) with the amide group were proposed for the ATP-Fe complex. In contrast, direct interaction with the phosphate group and indirect interaction with the amide group were observed for the AMP-Fe complex. The different interactions of the two complexes suggest an 'anti' conformation for the ATP-Fe complex and a 'syn' conformation for the AMP-Fe complex. The strong binding of Fe to ATP compared with AMP and the difference in the conformation of the ATP-Fe and the AMP-Fe complexes may be significant in the pathway of Fe release in mitochondria.
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PMID:A Raman study of the binding of Fe(III) to ATP and AMP. 144 15

The objective of this study was to prepare a new type water soluble bonding agent, methyl methacrylate (MMA)-p-styrene sulfonic acid copolymer (MS), and to investigate the effect of MS on bonding between resins and tooth substrates. MS is cross-linked with Ca2+ supplied by hydroxyapatite in a smeared layer on ground enamel and dentin and sticks to their surface. Samples were prepared by bonding an acrylic rod with MMA-TBB resin to ground enamel and dentin coated with an aqueous mixture of FeCl3 and 10 wt% MS. After immersed in water for 24 hrs, the tensile bond strength was measured. The bond strengths to both enamel and dentin were higher than 11 MPa and cohesive failure of cured MMA-TBB resin was observed in every case. This suggested that MS could adhere to tooth substrates with a new bonding mechanism different from the previously reported mechanism of the monomer interpenetration and polymerization.
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PMID:[Bonding of MMA-TBB resin to bovine tooth coated by poly (methyl methacrylate-co-p-styrene sulfonic acid)]. 248 5

The objective of this study was to prepare a new type water-soluble bonding agent, methyl methacrylate (MMA)-p-styrene sulfonic acid copolymer (MS), and to investigate the effect of MS on bonding between resins and tooth substrates. MS is cross-linked with Ca2+ released from ground enamel and dentin and could be immobilized on their surface. A sample was prepared by bonding an acrylic rod with a BPO-amine catalyzed self-curing resin to ground enamel and dentin coated with an aqueous mixture of FeCl3 and 10 wt% MS. After immersion in water for 24 hrs, the tensile bond strength was measured. The bond strength to both enamel and dentin was only 2 MPa and adhesive failure occurred at the interface between cured MS and self-curing resin. This suggested that cured MS could adversely effect the polymerization of self-curing resins. A second treatment of cured MS on the tooth surface with metallic cations was carried out to minimize the amount of free sulfonic acids in the MS disturbing radical formation in self-curing resin. The second treatment improved the bond strength to 6 MPa.
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PMID:[Bonding of MMA-BPO. DMPT resin to bovine tooth coated by poly (methyl methacrylate-co-p-styrene sulfonic acid)]. 248 6

The relationship between the structure of monomers with amide groups and their adhesiveness to tooth was investigated. The monomers used were methacrylamide (MA), p-methacryloxybenzamide (p-MBA), and 3,5-dimethacryloxybenzamide (3,5-DMBA). MA was commercially available. p-MBA and 3,5-DMBA were prepared from the reaction of methacryloyl chloride with p-hydroxybenzamide or 3,5-dihydroxybenzamide, respectively, in acetonitrile. The bovine enamel and dentin were etched with 10% citric acid -3% FeCl3 solution. The monomers were dissolved in MMA, and TBB-O was used as a polymerization initiator. The test samples were immersed in 37 degrees C water for 1 day, 1 month, or 3 months. Then the tensile bond strengths were measured. The bond strengths to enamel were almost the same, irrespective of the kinds of monomers after 1 day immersion. Although the bond strengths of MA (1.0%) and 3,5-DMBA (3.0%) decreased after 1 month immersion, those of MA (0.5%) and p-MBA (0.5%) did not decrease after 3 months immersion. There was no relationship between the bond strengths to enamel and the bending strengths of the resins. The bond strengths of 3,5-DMBA (1.0%) and 3,5-DMBA (3.0%) to dentin were about 5-7 MPa. The bond strengths of MA (0.5%) or MA (1.0%) decreased after 3 months or 1 month immersion, respectively. The bond strength of p-MBA (0.5%) did not decrease after 3 months immersion.
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PMID:[Studies on adhesion to tooth substrate. 5. The relationship between the structure of monomers and their adhesiveness]. 248 5

In this study the efficacy of the primer on adhesion of MMA (TBB-O) resin to dentin was investigated. The primer consists of two parts. One is 6% MTYA and 70% HEMA aqueous solution, and the other is 2% glutaraldehyde aqueous solution. As an etching agents, 10% citric acid-3% FeCl3 (10-3), 40% phosphoric acid, 10% citric acid, and 0.5 M EDTA were used. After etching, the two parts of the primer were mixed well and applied on the etched surface. Then MMA (TBB-O) resin or p-MBA/MMA (TBB-O) resin was applied on the treated surface. The tensile bond strengths after storage in 37 degrees C water were measured. It revealed that the primer treatment increased the bond strength despite the kind of etching agents. Though the thickness of the resin reinforced dentin was the same as that of demineralized dentin, it was not proportional to the bond strength. Then the durability of the adhesion to dentin treated with primer was examined by the thermal cycling tests. After 2000 thermocycles between 5 degrees C and 55 degrees C, the decrease in the bond strength was very small.
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PMID:[Studies on adhesion of MMA (TBB-O) resin to dentin. The efficacy of the primer treatment]. 249 Feb 3

The binding of Fe3+ to red cell membranes was studied in a system in which lipid peroxidation was proportional to Fe3+ concentration. Binding of Fe3+ was evaluated by labeling with 59FeCl3 and measurement of NMR water-proton relaxation times. Labeling with 59Fe showed that 95% of the Fe3+ was membrane bound at 100 microM FeCl3 in a 1.5 mg protein/ml membrane suspension. Both spin-lattice (T1) and spin-spin (T2) relaxation times decreased with increasing Fe3+ concentration. Addition of red cell membrane suspensions largely prevents the Fe3+ effect on relaxation times. Charge transfer to Fe3+ may occur at the membrane binding site with resultant decrease in the Fe3+ effect on water-proton relaxation times. These studies support the hypothesis that Fe3+ binds to the membrane and generates free radicals at the binding site.
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PMID:Binding of iron to human red blood cell membranes. 258 56


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