Showing papers on "Glutaraldehyde published in 1987"
••
TL;DR: This work enhances crosslinking through bridging of activated carboxyl groups with diamines and using glutaraldehyde to crosslink the epsilon-NH2 groups in collagen and the unreacted amines introduced by aliphatic diamines, which reduces tissue degradation and nearly eliminates humoral antibody induction.
Abstract: Glutaraldehyde crosslinking of native or reconstituted collagen fibrils and tissues rich in collagen significantly reduces biodegradation. Other aldehydes are less efficient than glutaraldehyde in generating chemically, biologically, and thermally stable crosslinks. Tissues crosslinked with glutaraldehyde retain many of the viscoelastic properties of the native collagen fibrillar network which render them suitable for bioprostheses. Implants of collagenous materials crosslinked with glutaraldehyde are subject long-term to calcification, biodegradation, and low-grade immune reactions. We have attempted to overcome these problems by enhancing crosslinking through bridging of activated carboxyl groups with diamines and using glutaraldehyde to crosslink the epsilon-NH2 groups in collagen and the unreacted amines introduced by aliphatic diamines. This crosslinking reduces tissue degradation and nearly eliminates humoral antibody induction. Covalent binding of diphosphonates, specifically 3-amino-1-hydroxypropane-1, 1-diphosphonic acid (3-APD), and chondroitin sulfate to collagen or to the crosslink-enhanced collagen network reduces its potential for calcification. Platelet aggregation is also reduced by glutaraldehyde crosslinking and nearly eliminated by the covalent binding of chondroitin sulfate to collagen. The cytotoxicity of residual glutaraldehyde--leaching through the interstices of the collagen fibrils or the tissue matrix--and of reactive aldehydes associated with the bound polymeric glutaraldehyde can be minimized by neutralization and thorough rinsing after crosslinking and storage in a nontoxic bacteriostatic solution.
413 citations
••
TL;DR: It is concluded that cell surface roughness may be an important parameter of cell adhesion and perhaps deformation and is made amenable to experimental study by the present approach.
40 citations
••
TL;DR: Sepiolite, a magnesium silicate, binds collagen resulting in a complex which has a gel-like structure when hydrated, and this material should be considered in the design of biomaterials.
40 citations
•
TL;DR: In tissue O2 is rapidly depleted both by respiration and the chemical demands of the glutaraldehyde-amine reactions during the cross-linking process, consistent with the synthesis of pyridine derivatives from glutarhyde-amine precursors in which the last step is an irreversible oxidation of dihydropyridine to pyridines.
39 citations
•
TL;DR: Both serial dilution and agar overlay techniques appear to be sensitive and effective methods for testing the toxicity of diffusible agents.
Abstract: Serial dilution and agar overlay techniques were used to compare the cytotoxicity of formocresol, 19% formaldehyde, 35% cresol, and 2.5% glutaraldehyde to human pulp fibroblasts. The maximum nontoxic concentration of each agent was determined to allow quantitative comparisons both of the agents tested and of the techniques used. Formaldehyde was found to be the major component of formocresol which is responsible for the cytotoxic effect on human pulp fibroblasts. Two and one-half per cent glutaraldehyde was 15-20 times less toxic than either formocresol or 19% formaldehyde. Cresol measured 40 times less toxic than formaldehyde or formocresol. Both serial dilution and agar overlay techniques appear to be sensitive and effective methods for testing the toxicity of diffusible agents.
36 citations
••
TL;DR: Bactericidal assays of 2% alkaline glutaraldehyde solution were carried out using Millipore membranes, and the rate of kill was compared with that of mycobacteria in suspension and on Penicylinder surfaces when using the methods recommended for the official tuberculocidal test.
Abstract: Bactericidal assays of 2% alkaline glutaraldehyde solution were carried out using Millipore membranes, and the rate of kill was compared with that of mycobacteria in suspension and on Penicylinder surfaces when using the methods recommended for the official tuberculocidal test. The rate of inactivation observed on the membrane filter surface was similar to that achieved using Penicylinders. The absence of visible colonies on the treated membranes provided a direct demonstration of sterility. The use of filter membranes in tuberculocidal tests provides a simple quantitative assay.
35 citations
••
TL;DR: Sensitive quantitative immunodetection is possible and, depending on the antiserum, peptides are readily detected in quantities down to 10 pg.
34 citations
••
TL;DR: The results support the idea that parathyroid cell variants occur during improper aldehyde fixation rather than that they express functional diversity, and heating specimens within sufficient short periods and enhancement of subsequent osmium fixation.
Abstract: Parathyroid cell variants, commonly observed in parathyroid glands fixed by immersion in glutaraldehyde, are believed to be the result of cyclic changes in the course of parathyroid hormone secretion. Immersion of bovine parathyroid glands in a mixture consisting of 1% glutaraldehyde, 1.5% formaldehyde, and 2.5% acrolein, followed by post-fixation in 1% osmium tetroxide, resulted in high uniformity with only one cell variant, whereas the same fixation procedure led to disruption of cell membranes and formation of cell variants in rat parathyroids. Parathyroid glands of both cattle and rats prepared by high-pressure quick-freezing and subsequent freeze-substitution contained only one cell variant. Excellent preservation of the ultrastructure of bovine and rat parathyroids, also exhibiting only one cell variant, was achieved by microwave irradiation in the presence of 2.5% glutaraldehyde in Na-cacodylate followed by post-fixation with OsO4 in Na-cacodylate or s-collidine, both containing Ca2+ and Mg2+. Use ...
34 citations
••
TL;DR: It is concluded that internal membranes in Methanobacterium thermoautotrophicum are artifacts arising during suboptimal fixation conditions.
Abstract: Methanogenic bacteria chemically fixed for electron microscopy contain internal membranes in the form of mesosomes and nucleoid vesicles, and the function of these membranes in methanogenesis and ATP synthesis has been speculated upon. Cells of Methanobacterium thermoautotrophicum fixed in phosphate-buffered 2.5% glutaraldehyde, 0.1% osmium tetroxide, or 0.5% glutaraldehyde – 2.5% formaldehyde always contain internal membranes. Cells freeze-fractured, freeze-substituted, or fixed in cacodylate-buffered 1% osmium tetroxide, 2.5% glutaraldehyde, or simultaneous glutaraldehyde–osmium lack internal membranes. We conclude that internal membranes in this species are artifacts arising during suboptimal fixation conditions.
31 citations
••
TL;DR: To test the reaction of a periarticular tissue to implanted pericardial membrane, substituting a segment of patellar ligament, a new method of cross-linking the collagenous matrix with glutaraldehyde is used, and there is no evidence of glutARaldehyde cytotoxicity.
Abstract: This study tested the reaction of a periarticular tissue to implanted pericardial membrane, substituting a segment of patellar ligament. Bovine pericardium was chemically purified and cross-linked with monomeric glutaraldehyde under pH, temperature and time conditions minimizing the polymerization of the cross-linking agent. Eight rats had both knee joint patellar ligaments excised. One side served as a control (simple suture), the other dissected ligament was replaced with a strip of pericardium. After 18 days and 12 weeks the dissected ligaments were analyzed by morphological methods. An unexpected fast ingrowth of cells and vessels was observed at 18 days. At 12 weeks new collagen deposits within pericardial patch were seen with striking biodegradation of the implant. Thus, using a new method of cross-linking the collagenous matrix with glutaraldehyde we see no evidence of glutaraldehyde cytotoxicity, as documented by our previous work.
30 citations
••
TL;DR: Findings indicate that the glutaraldehyde fixation method can be applied to mammalian collecting tubules for studying vasopressin stimulated Pdw and Purea and is functionally flexible and may be distinct from the water pathway.
Abstract: Using the in vitro microperfusion technique on isolated rat papillary collecting duct (PCD), we examined whether the glutaraldehyde-fixation method can be also applied to the mammalian collecting duct for preservation of the vasopressin-stimulated water and urea transport. Arginine vasopressin (AVP) at 10−9 mol/l increased diffusional water permeability (P
dw) from 101.9±10.76 to 283.3±16.67×10−7 cm2 s−1 (n=8,P<0.01) and urea permeability (P
urea) from 30.3±2.24 to 83.5±7.80×10−7 cm2 s−1 (n=8,P<0.01). Both parameters remained elevated after fixation with 0.1 mol/l glutaraldehyde even in the absence of AVP, with the values being 265.0±14.47 and 74.5±7.15×10−7 cm2 s−1, respectively. Glutaraldehyde fixation did not affect the basal levels ofP
dw orP
urea. Phloretin at 2.5×10−4 mol/l decreased glutaraldehyde-fixed AVP-stimulatedP
urea from 79.0±7.96 to 29.7±3.66×10−7 cm2 s−1 (n=4,P<0.01) and from 73.2±7.05 to 38.7±3.53×10−7 cm2 s−1 (n=4,P<0.01) when the drug was added to the lumen or to the bath, respectively. Phloretin also decreased glutaraldehyde-fixed non-stimulatedP
urea by 25–40%. However, this drug did not affect glutaraldehyde-fixedP
dw. These findings indicate that the glutaraldehyde fixation method can be applied to mammalian collecting tubules for studying vasopressin stimulatedP
dw andP
urea.P
urea fixed by glutaraldehyde is functionally flexible and may be distinct from the water pathway.
••
TL;DR: Immunocytochemical localization of 5-HT can be performed with good ultrastructural preservation of tissues and indicates that 5- HT in EC cells is stored mainly in secretory granules, with a small fraction of 5HT being localized outside the granules.
Abstract: Serotonin-like immunoreactivity (5-HT-LI) has been localized at the ultrastructural level in enterochromaffin (EC) cells of rat gastrointestinal tract Ultra-thin sections of tissues embedded in epoxy resin were incubated with 5-HT antisera and antibody binding sites were visualized with protein A-gold Three different antisera were compared and were shown to require different fixation regimens for optimal preservation of 5-HT-LI For one antiserum, tissues fixed in glutaraldehyde and osmium tetroxide could be used to demonstrate 5-HT-LI in EC cells Immunocytochemical localization of 5-HT can thus be performed with good ultrastructural preservation of tissues Quantitative evaluation of the intracellular distribution of 5-HT-LI was performed on EC cells from antrum, duodenum, and proximal colon, fixed in glutaraldehyde only In all three locations, the majority of the gold particles (90%) in EC cells were localized over the dense core of the secretory granules, while a minor fraction (10%) were localized in parts of the cytoplasm devoid of granules In EC cells fixed in glutaraldehyde and post-fixed in osmium tetroxide, 5-HT-LI was reduced by about 85%, although intracellular distribution was essentially the same as in cells fixed in glutaraldehyde alone The results indicate that 5-HT in EC cells is stored mainly in secretory granules, with a small fraction of 5-HT being localized outside the granules
••
TL;DR: Glutaraldehyde is an effective disinfectant against HAV: the infectious virus titer decreased by more than 3 log10 after 30 min using0.10% glutaraldehyde and within only 3 min using 0.50% glutARaldehyde.
••
TL;DR: With these methods, the serotonin and GRH neurons could be clearly and finely visualized and the reactive substances resulting from the avidinbiotin-peroxidase complex method were enhanced by osmication.
Abstract: With a view to improving the immunohistochemical technique for the demonstration of bioactive substances, i.e., neuropeptides and biogenic amines in the mammalian central nervous system, the procedures of immunoperoxidase methods were examined and some modifications for obtaining consistent results were developed.Brains of pharmacologically untreated animals were utilized as the material of the present study. The time through thoracotomy and preperfusion was reduced as much as possible. Perfusion fixation was performed at an increased rate, using a blood pump (hemolizer). The first fixative was a mixture of 4% formaldehyde, 0.2% picric acid, and 0.5% glutaraldehyde in phosphate buffer; the second was 4% formaldehyde and 0.2% picric acid in phosphate buffer acidified to pH6.5 with acetic acid; and the third was buffered formaldehyde solution. The osmotic pressure of all these fixatives was 1550-1650mOsM. Sections 25μm thick were produced on a Microslicer, followed by application of the freezing-thawing technique. The free-floating sections were incubated in a low concentration of antibody solution diluted by 0.5% Triton X-100 in phosphate buffer for a longer period than usual, under cool condition. The reactive substances resulting from the avidinbiotin-peroxidase complex method were enhanced by osmication. With these methods, the serotonin and GRH neurons could be clearly and finely visualized.
••
••
TL;DR: In this article, reaction de pentanedials avec des carbamoyl-2-, -3- and -4 piperidines: obtention respectivement d'octahydro dipyrido [1,2-a:1',2'-c] imidazolones-11, d' octaphylmethyl methano-1,5pyrido[1, 2-a] diazocine-1.3ones-6, and d'Octahydroid ethano]-1,4pyrid
Abstract: Reaction de pentanedials avec des carbamoyl-2-, -3- et -4 piperidines: obtention respectivement d'octahydro dipyrido [1,2-a:1',2'-c] imidazolones-11, d'octahydro methano-1,5pyrido [1,2-a] diazocine-1,3ones-6 et d'octahydro ethano-1,4pyrido [1,2-a] diazepine-1,3-ones-5
••
TL;DR: The oligosaccharides produced by β-galactosidase-1 was changed after immobilization onto porous silica gel (Merckogel) by crosslinkage with glutaraldehyde by increasing the maximum yield and the Km value was increased.
Abstract: The oligosaccharide-producing activity of β-galactosidase-1, one of the isomers of β-galactosidase (β-d-galactoside galactohydrolase, EC 3.2.1.23) from Bacillus circulans was changed after immobilization onto porous silica gel (Merckogel) by crosslinkage with glutaraldehyde. The reason for this modification was studied by treating the free enzyme with glutaraldehyde. Glutaraldehyde of 0.025% to 3% modified 40% to 90% of the free amino groups with or without intermolecular crosslinking. The maximum yield of oligosaccharides increased from 12% to 40% depending upon degree of modification, while native enzyme gave only 6% trisaccharides during hydrolysis of 127 mM lactose. The K m value for the enzyme treated with glutaraldehyde was also increased.
••
TL;DR: A copolymer with balanced hydrophilicity and hydrophobicity was synthesized by grafting butyl acrylate onto poly(vinyl alcohol) (PVA-g-BA).
Abstract: A copolymer with balanced hydrophilicity and hydrophobicity was synthesized by grafting butyl acrylate onto poly(vinyl alcohol) (PVA-g-BA). Films made from it had good urea permeability. After immobilization of the enzyme urease on the surface of it, the film was attached to the tip of an ammonia gas electrode to form an enzyme sensor. The sensor was able to detect urea in solution in the range of 6 to 600 mg/dL with a response time of about 5 min. It might be reused for over 100 times, and the reproducibility was very good. Therefore, it is very promising that this sensor may be commercialized for clinical use. The synthesis of PVA-g-BA was initiated with cerium ammonium nitrate, and the immobilization of urease was done by crosslinking with cyanuric chloride of glutaraldehyde. The former agent was proved to be more effective than the later. The amount of enzyme immobilized with the former were 26 and 13 times more than the one- and two-step methods with the latter, respectively.
••
TL;DR: In this paper, the composition of two glutaraldehyde solutions with different grades of purity was studied by HPLC, UV, J-H and 13C NMR spectroscopy.
Abstract: The composition of two glutaraldehyde solutions with different grades of purity was studied by HPLC, UV, J-H and 13C NMR spectroscopy. The reactions between various amino acids and the two glutaraldehyde solutions were investigated by UV spectrophotometry. The impurities in the most impure glutaraldehyde solution could be characterized with UV giving a 235 nm absorption, with HPLC as two peaks with retention times 3.36 and 5.78 min and with 13C NMR as small signals in the 102.7-94.9 ppm area. It is proposed that the two glutaraldehyde solutions give different reaction products with amino acids.
••
TL;DR: Sodium metabisulfite and glutaraldehyde were used alone and in combination to inactive Kunitz trypsin inhibitor (TI) in model systems and TI in lyophilized alkaline soy meal extract.
Abstract: Sodium metabisulfite and glutaraldehyde were used alone and in combination to inactive Kunitz trypsin inhibitor (TI) in model systems and TI in lyophilized alkaline soy meal extract. Reaction of glutaraldehyde (0.1 to 3.0%, based on total volume of the reaction mixture) with Kunitz TI (3 mg/ml buffer) at 25 C resulted in 60–75% reduction in activity. Treatment of soy meal extract containing 0.08 mg TI/mg at a concentration of 10 mg sample/ml buffer under similar reaction conditions reduced TI activity only 40%, however. A reaction temperature of 75 C had little additional effect on TI inactivation. On the other hand, sodium metabisulfite (0.05 to 1.0 mM) inactivated >96% Kunitz TI within 1 hr at 75 C and 75–94% of the TI in soy meal extract. The combination of 0.6 mM metabisulfite and 0.5% glutaraldehyde at 75 C inactivated >99% Kunitz TI, and combination of 0.6 mM metabisulfite and up to 3% glutaraldehyde inactivated 88% of TI in soy meal extract vs 91% inactivation with metabisulfite alone. Thus, metabisulfite plus glutaraldehyde inactivated Kunitz TI better than either one alone, while bisulfite alone best inactivated TI in soy meal extract. When the reactions were performed at neutral pH, protein solubility of 80% or better was retained.
••
TL;DR: Evidence is provided that glutaraldehyde might inhibit Cl− transport in the TAL by cross-linking amino acid residues of the proteins essential for halogen transport across this segment as well as evidence that the mechanism of Cl+ transport across the Tal is different from that of Na+ transport.
Abstract: In order to further characterize Cl− transport of the thin ascending limb of Henle's loop (TAL), we observed the effects of glutaraldehyde on Na+ and Cl− transport in hamster TAL perfused in vitro. We found that 0.1 mol/l glutaraldehyde added either to the lumen or to the bath caused a rapid irreversible reversal of the NaCl diffusion potential. This was mainly accounted for by an inhibition of Cl− permeability (10−7 cm2 s−1) from 93.51±8.39 to 14.89±3.91 (P<0.01,n=9). By contrast, Na+ permeability changed little from 34.18±3.27 to 26.56±2.74 (P<0.01,n=6). Glutaraldehyde treatment abolished the halogen-permselectivity of the TAL as determined by the voltage deflection seen upon ionic substitution. Permeabilities for Cl−, Br−, I−, and SCN− relative to Na+ were changed from 3.16±0.20, 3.22±0.19, 2.97±0.26 and 4.36±0.36 to 0.38±0.07, 0.35±0.06, 0.36±0.07 and 0.58±0.05, respectively. The effect of glutaraldehyde on the NaCl diffusion potential was dose-dependent in the range from 10−5 to 10−1 M. The effect was reversible at concentrations lower than 10−3 M. Glutaraldehyde did not affect the NaCl diffusion potential of the long-loop descending limb. These observations constitute additional evidence that the mechanism of Cl− transport across the TAL is different from that of Na+ transport. Glutaraldehyde might inhibit Cl− transport in the TAL by cross-linking amino acid residues of the proteins essential for halogen transport across this segment.
••
TL;DR: In this article, a wide range of immobilization procedures have been shown to stabilize the functions of photosynthetic materials, and the purpose of this work was to determine if the above procedures can be applied to submembrane fractions.
Abstract: A wide range of immobilization procedures have been shown to stabilize the functions of photosynthetic materials. The purpose of this work was to determine if the above procedures can be applied to submembrane fractions. Triton X-100-derived photosystem II submembrane fractions isolated from spinach were immobilized in a glutaraldehyde cross-linked albumin matrix. The optimal conditions were obtained in presence of 1 mM NaCl and 5 mM MgCl2. The treated membranes were less affected by long-term storage at 4°C, high pH and temperature, and strong light exposure. The results are discussed in terms of a diffusion barrier resulting from the immobilization matrix.
••
TL;DR: The preparation of 6- and 7-aryllumazines and the oxidation of these compounds by (immobilized) Arthrobacter M-4 cells containing xanthine oxidase is described.
••
TL;DR: In this article, the β-D-Galactosidase from E. Coli was crosslinked using glutaraldehyde and two bisimidoesters, which gave higher activity than the native enzyme.
Abstract: β-D-Galactosidase fromE. Coli was crosslinked using glutaraldehyde and two bisimidoesters. With glutaraldehyde and dimethyl adipimidate (DMA), it is possible to obtain preparations having higher activity than the native enzyme. Glutaraldehyde and DMA gave preparations showing enhanced thermal stability. The preparation crosslinked with DMA, when used for continuous hydrolysis of lactose in milk, was found to be significantly better than the native enzyme.
••
TL;DR: Results indicate that an application of the cryofixation method is useful for improving resolution and specificity in immunocytochemical postembedding staining.
Abstract: An applicable method of cryofixation to immunocytochemistry was examined. Fresh tissue blocks of rat pancreas and parotid gland were quickly frozen by the metal contact method using liquid helium and freeze-substituted with one of the following media kept at -80°C for 36hr; pure acetone, 0.1% glutaraldehyde (anhydrous) in acetone, approximately 0.2% paraformaldehyde in acetone, and 10% acrolein in acetone. After freeze-substitution fixation, tissue blocks were embedded in Araldite mixture. Thin sections mounted on nickel grids were processed for immunocytochemical localization of amylase according to the multiple-step protocol of the protein A-gold immunostaining method by Bendayan and Duhr (4). They were then postfixed with 2.5% glutaraldehyde in PBS and stained with uranyl acetate and lead citrate for electron microscopy. Good results were obtained from the materials substituted with glutaraldehyde or paraformaldehyde in acetone. The ultrastructural features of the cells were preserved well, similar to those in the materials substituted with OsO4 in acetone except for negative images of the membranous structures. Secretory granules, condensing vacuoles, and Golgi cisterns were labeled well with immunogold. Labeling density was much higher in the present materials than in those processed by conventional chemical fixation, and the intensity of labeling increased in proportion to increasing electron density of the materials contained within individual subcellular compartments. These results indicate that an application of the cryofixation method is useful for improving resolution and specificity in immunocytochemical postembedding staining.
••
TL;DR: Glutaraldehyde has been found to be a better inactivating agent for the preparation of a safe pertussis suspension as it considerably reduced the histamine sensitizing activity of pertussi toxin.
••
TL;DR: Ca 2+ and Mg 2+ alone or in combination reduce swelling of RER, extraction of cellular material and loss of subcellular compartments, such as secretory granules, under optimal conditions but Ca 2+ provokes formation of dark and light cells accompanied by loss ofSubcellular components when used in low concentration during osmication.
•
25 Sep 1987
TL;DR: In this article, a liquid sterilizing composition with a broad activity spectrum, which as the active componeents contains phenoxy ethanol and, in addition, glutaraldehyde, formaldehyde, or glyoxal, was described.
Abstract: The invention concerns a liquid sterilizing composition with a broad activity spectrum, which as the active componeents contains phenoxy ethanol and, in addition, glutaraldehyde, formaldehyde or glyoxal, especially glutaraldehyde. The composition according to the invention contains as an activated solution 0.15 to 15 % by weight of phenoxy ethanol and 0.03 to 8 % by weight of glutaraldehyde, formaldehyde or glyoxal, as well as further per se known adjuvants.
•
TL;DR: It was concluded from these experiments that buffering GA, increasing its concentration, and applying it for longer periods, all enhance the degree of fixation; only stronger solutions increase the depth of fixation.
Abstract: The effects of time, concentration, and pH on glutaraldehyde ( GA) fixation were studied in vitro using 2 model systems: coIlagen-BSA gels as simulations of cell cytoplasm and enzyme activity in treated pulp tissue. The former system demonstrated that GA is most effective when buffered, and that its penetration is self-limiting. In general, concentration proved more a factor in the depth of penetration than did time. It was concluded from these experiments that buffering GA, increasing its concentration, and applying it for longer periods, all enhance the degree of fixation; only stronger solutions increase the depth of fixation. Practically, the data suggest that clinical treatment might involve using buffered glutaraldehyde -- either at 4% for 4 rain or 8% for 2 rain.
••
TL;DR: The results show that parathyroid cell variants arise during immersion fixation and that aldehydes, buffers and temperature are important factors for provoking parathyroid cell variants.
Abstract: Parathyroid glands of cattle, dogs, cats, mice and rats were immersed in glutaraldehyde or mixtures consisting of glutaraldehyde, formaldehyde and acrolein in either Na-phosphate, Na/K-phosphate or Na-cacodylate buffer, and postfixed with OsO4 in the same buffers or, alternatively, in s-collidine.