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)

Sixty ready-to-cook broiler carcasses obtained from several local supermarkets were tested for the presence of Yersinia enterocolitica and other Yersinia species. In the present study, the authors used two enrichment broths, yeast-extract/rosebengal-bile oxalate sorbose (YER-BOS) and phosphate-buffered saline with a postenrichment KOH treatment (PBS-KOH), and two plating media, cefsulodin-irgasan-novobiocin (CIN) and pectin agar. Yersinia organisms were found on 34 of 60 carcasses (56.7%) and Y. enterocolitica, on 16 of 60 carcasses (26.7%). There was no significant difference between CIN and pectin agar; however, PBS-KOH yielded a significantly higher (P less than or equal to .05) detection rate than YER-BOS, regardless of the plating media used. In addition to Y. enterocolitica, Y. frederiksenii and Y. intermedia were also isolated from the market broilers. None of the Y. enterocolitica isolates were found to be presumptively virulent.
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PMID:The presence of Yersinia enterocolitica and other Yersinia species on the carcasses of market broilers. 234 28

Endogenous testosterone concentrations in rat seminiferous tubules were measured in relation to different stages of the cycle of the seminiferous epithelium. For this purpose, the seminiferous tubules were mechanically separated from the interstitial tissue on a cooled (1 degree C) petri dish under a stereomicroscope without added medium. After recognition of the stages of the cycle by transillumination, the specimens were rapidly transferred by dry forceps into test tubes for testosterone radioimmunoassay. The results of the dry dissection method were compared with measurements on tubules that were kept after separation in phosphate buffered saline (PBS, pH 7.4), in order to reveal the possible leakage of testosterone from the tubules. The maximal concentration of testosterone per unit length of seminiferous tubule was found in stages VII and VIII of the cycle (288 +/- 60 fmol/cm, mean +/- SEM, n = 12), and the minimal in stages IX-XII (219 +/- 57 fmol/cm, P less than 0.01). If the levels were correlated with unit volumes of the seminiferous tubules, identical concentrations of testosterone (521-542 fmol/mm3, approx. 500 nmol/l) were found in the different stages of the cycle. Despite the similarity of testosterone concentrations in the different parts of the seminiferous tubules the local concentrations of biologically active (i.e. free) testosterone may be modulated by extracellular and intracellular androgen binding components.
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PMID:Testosterone micromilieu in staged rat seminiferous tubules. 239 68

Human alpha 2-macroglobulin (alpha 2M) was eluted as a single nondispersed peak from a TSK-G4000SW size exclusion chromatography column equilibrated in 20 mM-sodium phosphate/100 mM-NaCl, pH 7.2 (PBS). The void volume and total accessible volume of the column were 6.08 ml and 14.42 ml. The elution volume (Ve) of native alpha 2M was 9.20 +/- 0.04 ml. The Ve was altered minimally by changing the ionic strength or adding ethanol to the equilibration buffer. Ternary alpha 2M-trypsin, containing 2 mol of proteinase/mol of inhibitor, and alpha 2M-methylamine failed to be eluted in well-defined peaks when the column was equilibrated in PBS. The majority of either preparation was recovered slowly at Ve values greater than 14.5 ml, reflecting significant nonideal interactions with the support structure. Addition of 10% ethanol or increased ionic strength in the equilibration buffer independently caused either form of reacted alpha 2M to be eluted in a distinct peak at decreased Ve, suggesting that the nonideal interactions included hydrophobic and electrostatic adsorption. When the equilibration buffer was 80 mM-sodium phosphate/320 mM-NaCl, pH 7.2, partial resolution of ternary alpha 2M-trypsin and alpha 2M-methylamine was obtained with a single column run. The Ve values of ternary alpha 2M-trypsin and alpha 2M-methylamine in this buffer were 13.15 +/- 0.08 ml and 11.94 +/- 0.14 ml, respectively. The Ve of native alpha 2M was 8.84 +/- 0.03 ml. The resolving capacity of TSK-G4000SW was exploited to purify native alpha 2M rapidly and efficiently from solutions that contained significant amounts of either ternary alpha 2M-trypsin or binary alpha 2M-trypsin (1 mol of proteinase/mol of inhibitor). This purification was complete within the limits of sensitivity of denaturing and nondenaturing polyacrylamide-gel electrophoresis. alpha 2M-plasmin was well resolved from native alpha 2M. The Ve of alpha 2M-plasmin was 12.88 +/- 0.32 ml in 80 mM-sodium phosphate/320 mM-NaCl, pH 7.2. A number of procedures were used to prepare solutions with up to 90% binary alpha 2M-trypsin. The Ve of binary alpha 2M-trypsin in these various solutions was intermediate between the values of native alpha 2M and ternary alpha 2M-trypsin. The conformations of binary and ternary complex, as reflected by mobility in nondenaturing electrophoresis, were identical, confirming previous results. Finally, in the binary alpha 2M-trypsin complex, the single trypsin cleaved more than two, and as many as all four alpha 2M subunits.
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PMID:Purification and characterization of human alpha 2-macroglobulin conformational variants by non-ideal high performance size-exclusion chromatography. 242 74

Idiotype/anti-idiotype networks have been extensively investigated in such conventional animal models as the mouse and the rabbit. However, systems of veterinary interest have remained largely unexplored. A monoclonal target idiotype, with which to begin such studies in cattle was provided by LHRB 19.17 an interspecific bovine x mouse hybridoma. This hybridoma was constructed by the fusion of supramammary lymph node cells from S. agalactiae-immunized lactating Holsteins with the Ig synthesis-permissive established cell line, SP 2/0. Two collections of monoclonal anti-idiotype antibodies were generated by fusion of spleen cells from LHRB 19.17-immunized Balb/c or A/J mice immunized with the monoclonal bovine idiotype, LHRB 19.17. Many of the anti-idiotypes inhibited binding of LHRB 19.17 to S. agalactiae, but only one, LHRAID 2.71, proved to be an internal image of a S. agalactiae epitope. Immunization of C/D outbred rats by priming with 100-300 micrograms of LHRAID 2.71 emulsified in CFA followed by a 300 micrograms boost at day 32 elicited anti- S. agalactiae antibody in 4/4 animals tested. Similarly, the injection of two lactating Holsteins with the anti-id resulted in the production of anti- S. agalactiae antibody in serum and milk. In both rats and cattle, the administration of the antigen-mimicking anti-idiotype induces the appearance of S. agalactiae-reactive horseradish peroxidase-streptavidin conjugate; LHRBs, interspecific bovine x mouse hybridomas secreting bovine Ig; LHRAID.X, monoclonal anti-bovine idiotype antibodies derived against LHRB 19.17; PBS, phosphate buffered saline; PBS/BSA, PBS containing 0.1% bovine serum albumin: antibody [AB3] that competes with LHRB 19.17 [AB1] for binding to LHRAID 2.71 [AB2]. It should also be noted that the immunization of C/D rats with S. agalactiae does not result in the appearance of idiotypes which compete with LHRB 19.17 for binding to LHRAID 2.71. We have concluded that immunization of two widely divergent species with the antigen mimicking LHRAID 2.71 induced a S. agalactiae-reactive idiotype which was not detectable in the immune response of rats to S. agalactiae.
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PMID:Comparative idiotype network interactions: antigen mimicry by an anti-bovine idiotype monoclonal antibody in rats and cattle. 245 77

The interaction of cationic anesthetics with biological membranes and the resulting alterations of membrane electrokinetic properties continue to be of current interest. The present study was designed to examine the effects of procaine hydrochloride (PRHCL) on the mobility of human red blood cells (RBC); electrophoretic measurements were made on RBC suspended in phosphate-buffered saline (PBS, pH = 5.0, 7.4, or 9.2), autologous plasma or 3 g% dextran T70/PBS (pH = 7.4), with PRHCL concentrations from 8 x 10(-6) to 8 x 10(-2) M. Low concentrations of PRHCL (8 x 10(-5)-8 x 10(-3) M) significantly (p less than 0.001) increased RBC mobility, with a maximal increase of 8.2% at 8 x 10(-4) M. Conversely, a higher PRHCL concentration (8 x 10(-2) M significantly (p less than 0.001) decreased RBC mobility. Both glutaraldehyde fixation and lipid extraction abolished any PRHCL-induced increase in RBC mobility; the observed increases in mobility for normal cells are, thus, consistent with a mechanism based on expansion of the RBC membrane glycocalyx. Microelectrophoretic methods were also used to study the effect of PRHCL (8 x 10(-4) and 8 x 10(-2) M) on RBC membrane calcium binding, with the results indicating that PRHCL competes with calcium for neuraminate binding sites. We conclude that the observed changes in RBC electrokinetic properties reflect incorporation of PRHCL into the RBC membrane; such changes may be of importance in modulating cell-cell interactions.
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PMID:Effect of procaine hydrochloride on the electrophoretic mobility of human red blood cells. 248 Jan 83

Enzyme-linked immunoelectrotransfer blot (EITB) using crude worm antigen of adult Paragonimus westermani was performed for human patients sera to identify the species-specific components. Crude antigen was obtained by homogenizing and centrifuging 24-week old adult worms at 10,000 rpm for 60 minutes in phosphate buffered saline (PBS, pH 7.2) containing phenyl methyl sulfonyl fluoride (PMSF). Gradient sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was performed and blotted electrophoretically onto a sheet of nitrocellulose paper. The sheet was cut into strips and exposed to sera diluted 1: 200 with PBS. SDS-PAGE showed 26 protein bands ranging 229 to 10 kDa. Of them 229, 91, 60, 50, 35-31, 27, 25, 21, 17, 11 and 10 kDa components showed positive reaction with serum antibody of patients with P. westermani. Sera of patients infected with Clonorchis sinensis reacted with 35-31, 19, and 11 kDa bands. Human sera from cysticercosis and diphyllobothriasis cases showed non-specific cross reactions with 229, 35-31, 27, 25 and 17 kDa bands. Protein bands of 91, 60, 21 and 10 kDa showed strong positive reaction without cross reactions with sera from other helminthic infections.
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PMID:Demonstration of species-specific and cross reactive components of Paragonimus westermani crude worm antigen by EITB. 248 66

A method for detection of anticardiolipin (ACL) antibodies with enzyme-linked immunosorbent assay was developed. Microtitre plates were coated with cardiolipin at a concentration of 20 micrograms/ml by evaporation under 4 degree centigrade overnight. Non-specific binding of diluted sera was eliminated by blocking of plates with 10% fetal calf serum in phosphate buffered saline (FCS/PBS) for 2 hours at room temperature. Sera (50 microliters/well) at a dilution of 1:100 were incubated for 2 hours at room temperature. Horseradish peroxidase conjugated rabbit anti-human IgG, IgM, IgA at a dilution of 1:2000, 1:1000, 1:500 respectively was added to the wells, and incubated for one and half hours at room temperature. The results were read at 490nm after incubation with substrates at 37 degree centigrade. 85 patients with systemic lupus erythematosus (SLE), 45 with rheumatoid arthritis (RA), 25 with progressive systemic scleroderma (PSS), and 18 primary Sjogren's syndrome were tested. The frequency of ACL antibody in SLE (48%) was much higher than that in RA (11%), PSS (12), SS (5.5). Three isotypes of ACL (IgG, IgM, IgA) were detected in the study with predominance of IgG isotype. ACL antibody was significantly associated with thrombosis, cutaneous vasculopathy, thrombocytopenia, and spontaneous abortion in patients with SLE. Strong relationship between ACL antibody and lupus anticoagulant was found. There was no correlation between ACL and anti-DNA antibodies, nor was ACL and VDRL test. The level of ACL antibody could be reduced by use of corticosteroids.
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PMID:[Measurement of anticardiolipin antibodies and its significance in systemic lupus erythematosus]. 250 Mar 15

Small unilamellar liposomes, composed of dioleoylphosphatidylethanolamine (DOPE) and oleic acid (OA), prepared by sonication, were incubated in the presence of human plasma at 37 degrees C. The release of entrapped calcein after 8-h incubation was about 15% in plasma, compared with about 70% in phosphate-buffered saline under the same conditions. In contrast, dioleoylphosphatidylcholine (DOPC)/OA liposomes under the same conditions release about 70% in plasma and only 10% in PBS. Total release of calcein from the DOPE/OA liposomes was observed in a PBS solution containing bovine serum albumin, and the release was completely blocked by preincubation of the liposomes with plasma. These results indicate that the unstable DOPE/OA liposomes are stabilized by incubation with plasma. The stabilization process was very fast, being completed within 1 min. Only relatively small liposomes (d less than or equal to 200 nm) were completely stabilized by plasma; larger liposomes were progressively less stabilizable. SDS-polyacrylamide gel electrophoresis of liposomes which had been incubated with plasma and then washed indicated that several proteins were tightly associated with liposomes. Using liposomes containing [14C]OA, it was found that about 70% of the original OA was extracted after 1-h incubation with human plasma at 37 degrees C. Thin-layer chromatographic analysis of the plasma-treated liposomes showed the presence of the plasma lipids in the liposomes. These results suggest that liposomes composed of DOPE/OA are stabilized by protein and/or lipid components from human plasma and that the composition of the liposomes is altered. The mechanism of stabilization is discussed in terms of the surface pressure of small vesicles with a high degree of curvature.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Small, but not large, unilamellar liposomes composed of dioleoylphosphatidylethanolamine and oleic acid can be stabilized by human plasma. 261 Dec 8

Lucilia Caesar larvae (LCL) are used as live fish bait by anglers. Five cases of asthma and rhinoconjunctivitis following exposure to LCL are reported. Three had work-related asthma as they were working on a fish bait farm or shop and two had asthma when they went fishing. In one subject exposure to LCL caused asthma, rhinoconjunctivitis and contact urticaria. In four subjects peak expiratory flow rate (PEFR) was monitored during exposure to LCL. In three out of four subjects there was evidence of LCL-related asthma. In one subject it was not possible to record PEFR during exposure to LCL, as he had not gone fishing since 1985. Two extracts of LCL were prepared: one was the PBS (phosphate-buffered saline) washing fluid of LCL, the other was the PBS extract of homogenized LCL. Positive cutaneous prick tests to both LCL extracts were detected in three out of four symptomatic subjects. Specific IgE against both LCL extract antigens were found by the RAST method in four out of five subjects with LCL-related asthma. One subject had both negative skin tests and RAST. Specificity and potency of LCL-IgE binding was shown by RAST inhibition method performed on the serum pool of four patients with positive RAST results. Significant inhibition of more than 50% by LCL washing fluid at a dilution extract was found at a dilution of 1:10 and by homogenized LCL extract at a dilution of 1:100. No significant inhibition of LCL-IgE binding by dermatophagoides, parietaria and milk antigens was found. This study demonstrated that LCL emanations are potent sensitizers and elicit IgE-mediated asthma.
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PMID:[Asthma caused by Lucilia Caesar larvae: clinical and immunologic study]. 263 Aug 95

Cigarette smoke has been reported to contain free radicals and free radical generators in both the gas and particulate phases. Studies in our laboratory have shown that both cigarette smoke condensate (CSC) and smoke bubbled through phosphate buffered saline solution (smoke-PBS) increased sister chromatid exchanges (SCE) in Chinese hamster ovary cells in a dose-dependent manner. Since oxygen free radicals have been shown to cause SCEs and other chromosomal damage, we investigated the role of these radicals in the induction of SCEs by CSC and smoke-PBS. Addition of the antioxidant enzymes catalase and superoxide dismutase or the oxygen-radical scavenger ascorbic acid failed to reduce the SCE frequency in the presence of either CSC or smoke-PBS. Additional studies indicated that the quantity of hydrogen peroxide produced in CSC or smoke-PBS is too small to account for the observed SCE induction. It appears, therefore, that SCE induction by CSC or smoke-PBS does not involve the participation of oxygen free radicals.
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PMID:Role of oxygen free radicals in the induction of sister chromatid exchanges by cigarette smoke. 264 5


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