Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P30536 (PBS)
 9,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Dextran sulfate aggregates several enteroviruses depending not only on the pH, the ionic strength of the medium, but also on the protein content of the fluids and on strain specificities of the viruses. The aggregation effect was measured by filtration experiments, by sedimentation in the ultracentrifuge and by electron microscopy. The well known inhibiting effect of dextran sulfate on plaque formation may be due to its aggregating effect: A very strong inhibition of the release of matured virions from the infected cells is observed in medium containing dextran sulfate, whereas the adsorption process is inhibited much less compared with PBS controls. The maximal effect on virus aggregation, plaque size and virus release is observed at the same concentration of dextran sulfate.
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PMID:Strain-specific aggregation of enterovirus by dextran sulfate. 617 8

We studied two patients with an axonal type of polyneuropathy, epidermolysis, and IgM kappa plasma cell dyscrasia. The IgM kappa was deposited in the dermis, was absorbed from the serum by axonal micelle preparations, and was precipitated with chondroitin sulfate in highly purified agarose in 0.15 M NaCl with 0.01 M phosphate buffer, pH 7.8. In contrast, we found none of these abnormalities in three patients with IgM plasma cell dyscrasia and demyelinating neuropathy. Of 78 other macroglobulinemic serum samples from patients without neuropathy, 7 precipitated with a sulfated polysaccharide. This reaction occurred at low ionic strength, 0.05 M barbital buffer, pH 8.1, but did not occur in the higher ionic strength of 0.01 M phosphate with 0.15 M NaCl (PBS). The interaction of the IgM with chondroitin sulfate at relatively high ionic strength could cause both the axonal polyneuropathy and the epidermolysis.
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PMID:Monoclonal IgM kappa antibody precipitating with chondroitin sulfate C from patients with axonal polyneuropathy and epidermolysis. 629 26

Spontaneously existing and chemically induced micronuclei were isolated from mouse blood. 50 microliters of cardiac blood was diluted with PBS and centrifuged. After this, the cell pellet was subjected to hypotonic treatment, fixed with acetic acid-methanol (1:3), and the lysate was filtrated through a 2-microns polycarbonate nucleopore membrane. Isolated micronuclei were air-dried on a glass slide and subjected to fluorescence in situ hybridization (FISH) using a mouse centromeric gamma satellite probe. Approximately half of the micronuclei isolated from vehicle control mice showed centromere signal(s). In these preliminary studies, the proportion of centromere-positive micronuclei was increased by treatment with spindle poisons (colchicine and vinblastine sulfate), decreased only slightly by 1-beta-D-arabinofuranosylcytosine, and was generally unaffected by mitomycin C.
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PMID:Isolation of micronuclei from mouse blood and fluorescence in situ hybridization with a mouse centromeric DNA probe. 751 3

To construct the strategy for delivery systems that can control in vivo disposition of antisense oligonucleotides, we studied the stability and basic pharmacokinetic characteristics of oligonucleotides. Decathymidylic acid (T10), a model oligodeoxynucleotide, and its derivatives, 5'-biotin-T10) and 3'-methoxyethylamine 5'-biotin-T10 (3'M5'B-T10), containing phosphoroamidate modification at 3'- and/or 5'-terminal internucleoside linkages, were synthesized. In phosphate-buffered saline (PBS, pH 7.4) containing 10% mouse serum, unmodified T10 was degraded with a half-life of 45 minutes; the degradation half-lives of 5'B-T10 and 3'M5'B-T10 were 11 and 30 h, respectively. In mouse whole blood, 3'M5'B-T10 was relatively stable, and 45% remained intact after 1 h incubation. After intravenous injection of [3H]3'M5'B-T10 into mice at a dose of 1 mg/kg, the radioactivity was rapidly cleared from plasma with a half-life of 2 minutes and accumulated in the kidney, liver, and gallbladder. About 30% of the dose was excreted in the urine within 60 minutes. A much more rapid degradation of [3H]3'M5'B-T10 was observed in vivo than expected from in vitro experiments: more than 90% of the radioactivity in plasma was degradation product at 2 minutes after injection. These results suggested that enzymatic degradation occurred in some compartments in addition to the blood pool. The apparent urinary excretion clearance of [3H]3'M5'B-T10 was close to that of inulin, whereas the apparent hepatic uptake clearance was much greater than that of inulin and comparable to that of dextran sulfate, which is taken up by the liver by scavenger receptors for polyanions.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Stability and pharmacokinetic characteristics of oligonucleotides modified at terminal linkages in mice. 758 Jan 15

Anti-A reagent for the detection of the relevant antigen in human red cells and saliva has been developed. The reagent is prepared by dissolution of purified Vicia villosa lectin in the serum of group AB or B diluted 8 times with PBS. This solvent appreciably improves the anti-A selectivity of lectin and is used for titration. Purification of lectin by ammonium sulfate precipitation is described. The reagent agglutinates group A red cells in the minimal lectin concentration of 2.5 to 10 micrograms/ml and does not agglutinate group 0 and B red cells in concentration 10 mg/ml. Moreover, the reagent is fit for the detection of antigen A in traces of blood and saliva by the absorption-elution method.
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PMID:[The preparation of an anti-A reagent from the lectin of hairy vetch (Vicia villosa) for detecting antigen A in human erythrocytes and saliva]. 772 54

A new method for purifying IgG was adapted for use with chicken serum. Chicken serum was mixed with caprylic acid, precipitated with ammonium sulfate, and dialyzed against PBS. Analysis by SDS-PAGE and Western blot confirmed successful purification of chicken IgG. Large quantities of highly purified IgG were easily obtainable for use in immunological investigations or for labeling. This technique is rapid, inexpensive, and simpler to perform than traditional ion exchange or gel filtration chromatography.
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PMID:Simple method to purify chicken immunoglobulin G. 793 78

The active encapsulation of doxorubicin (DOX) into fluorinated liposomes, the stability of these liposomes with respect to encapsulated DOX release in buffer and in human serum, and their H+/Na+ membrane permeability have been investigated and compared to those of their conventional hydrogenated analogues. These fluorinated liposomes are made from highly fluorinated phosphatidylcholines and contain a fluorinated core within their membrane. We found that the presence of this fluorinated core is not a barrier for the active encapsulation of DOX. Efficient (> 90%) and stable loading could be achieved using a transmembrane ammonium sulfate or even, in the absence of Na+, a transmembrane pH gradient. The higher H+/Na+ permeability found for the fluorinated membranes, as compared to conventional ones, is responsible for the lower stability observed for the DOX-loaded fluorinated liposomes when incubated in a physiological buffer (PBS) or in human serum. It is also noticeable that the retention of DOX is increased in human serum and for the liposomes whose membranes are in a gel or in a semi-fluid semi-gel state at 37 degrees C.
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PMID:Fluorinated phosphatidylcholine-based liposomes: H+/Na+ permeability, active doxorubicin encapsulation and stability, in human serum. 807 42

Current bacterins provide only partial protection against morbidity and mortality in swine following infection by Actinobacillus pleuropneumoniae. We compared the efficacy of a cell-free concentrate from mid-log phase growth cultures of Actinobacillus pleuropneumoniae (APP) serotype 1 to four commercial bacterins. This cell-free preparation contained carbohydrate, endotoxin, and protein, and had hemolytic and cytotoxic activity. Sodium dodecyl-sulfate polyacrylamide gel electrophoresis analysis indicated the presence of one major 110,000-molecular-weight protein. This protein band also stained by the periodic acid Schiff method, indicating the presence of carbohydrate. Cell-free concentrates of APP serotypes 5 and 7 had identical profiles following electrophoresis and staining with either Coomassie blue for protein or Schiff reagent for carbohydrate. Lipopolysaccharide profiles for the cell-free concentrates of serotypes 1 and 5 were semi-rough while the LPS profile for serotype 7 was smooth. Five A. pleuropneumoniae-free SPF pigs per group were vaccinated on days 0 and 21 with cell-free concentrate of serotype 1 plus adjuvant, or one of four commercial bacterins according to the manufacturer's directions. Control pigs were vaccinated with PBS mixed with adjuvant. All pigs were challenged intranasally on day 35 with serotype 1 and necropsied on day 50. Protection was greatest in the cell-free concentrate group, as compared with all other groups, in that no deaths occurred, clinical scores were less severe, and percent lung affected was significantly reduced (P < 0.05). In addition, whole-cell ELISA titers were significantly increased (P < 0.05) postvaccination in the cell-free concentrate group, and postvaccination and postchallenge sera neutralized the hemolytic activity of the cell-free concentrate from serotypes 1 and 5 (P < 0.05), as compared with all other groups. No serum neutralization to the hemolysin of serotype 7 was observed. Immunoblot analysis using antisera derived from gnotobiotic pigs indicated that the cell-free vaccine generated a response that was identical to the response observed following live challenge. Similar, but not identical, responses were observed when antisera generated against the bacterins was used. This study indicates that an acellular vaccine containing multiple virulence factors can provide complete protection from mortality and significantly reduced morbidity to homologous challenge.
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PMID:The importance of secreted virulence factors in Actinobacillus pleuropneumoniae bacterin preparation: a comparison. 829 54

The mitochondrial DBI receptor complex (mDRC; previously called the peripheral benzodiazepine receptors) is linked to the production of neurosteroids such as pregnenolone sulfate, dehydroepiandrosterone sulfate, and others. In order to gain further information as to the function of the mDRC in the brain, we have constructed and tested both in vitro and in vivo a novel series of ligands, 2-arylindole-3-acetamides. The SAR studies detailed herein delineate some of the structural features required for high affinity binding to the mDRCs. In most cases the new ligands were prepared by use of the Fischer indole synthesis. Variations in the length and number of the alkyl groups on the amide nitrogen were probed together with the effects of halogen substituents on one or both of the aryl rings. Some ligands were also synthesized for study which represent conformationally constrained versions of the parent structure. Broad screening studies revealed these indoleacetamides to be highly selective for the mDRC, since they failed to bind with any significant affinity to other receptor systems. Some of the ligands were found to exhibit Ki values in the low nanomolar range for the mDRC as measured by the displacement of [3H]4'-chlorodiazepam. A subset of these ligands was also shown to stimulate pregnenolone formation from the mitochondria of C6-2B glioma cells with an EC50 of about 3 nM. In animal experiments ligands selected for further study were found to exhibit antineophobic effects, in spite of the fact that they exhibit no direct action on GABAA receptors. Consequently, it is postulated that these ligands owe their action to an indirect modulation of GABAA receptor function, presumably by stimulation of neurosteroid production and release from glial cells, followed by neurosteroid modulation of GABA's action on the chloride ion channel conductance of GABAA receptors.
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PMID:Chemistry, binding affinities, and behavioral properties of a new class of "antineophobic" mitochondrial DBI receptor complex (mDRC) ligands. 841 Oct 7

The aim of this study was to examine the effects of biglycan, a small chondroitin sulfate proteoglycan with neurotrophic activity, on memory and reinforcement upon unilateral injection into the region of the nucleus basalis magnocellularis (NBM). In experiment 1, rats with chronically implanted cannulas were injected with biglycan and tested on the uphill avoidance task, which involves punishment of a high-probability turning response on a tilted platform (negative geotaxis). Immediately after the training trial, that is, after a tail-shock was administered upon performing the response, rats received one microinjection (0.5 microliter) of substance P (SP) in a reference dosage of 0.74 pmol or biglycan (doses ranging from 1.3 to 1300.0 nmol) into the NBM region. When tested 24 h later, rats treated with SP (0.74 pmol) or biglycan (2.1 and 2.6 nmol) had significantly longer uphill latencies than vehicle (PBS) controls, indicative of superior learning of the avoidance response. In experiment 2, a test for possible proactive effects of post-trial biglycan on performance during the retention trial was performed. Furthermore, the uphill avoidance task was combined with a conditioned place preference task to assess possible reinforcing effects of biglycan. Rats were injected with either 2.6 or 130.0 nmol biglycan immediately after the training trial of the uphill task. One control group received 2.6 nmol biglycan 5 h after the trial, a second group was sham-operated. Additional groups were included which received biglycan (2.6 or 130.0 nmol), SP (0.74 pmol) or PBS after the training trial but no tail-shock.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Facilitation of learning following injection of the chondroitin sulfate proteoglycan biglycan into the vicinity of the nucleus basalis magnocellularis. 851 29


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