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)

An antigen was purified from Mycobacterium tuberculosis H37Ra culture filtrate by immunoabsorbent affinity chromatography with CNBr-activated sepharose 4B column coupled with pooled gamma-globulin fraction from patients with active tuberculosis. The column was washed extensively with PBS and eluted with 3M sodium thiocyanate. Peak fractions were pooled and used as coating antigen in an ELISA. Sera from 86 normal subjects and 54 patients with active tuberculosis were tested against the immunoabsorbed antigen by ELISA with biotin-conjugated anti-human globulin and avidin-peroxidase reagents. At a selected "cut-off" dilution of 320, 49 (91%) of 54 sera from active cases and 8 (9.3%) of 86 sera from normal subjects gave positive test results--a sensitivity and specificity each of 91%, compared with our previous results of sensitivity 75% and specificity 83% with PPD as antigen.
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PMID:Improved ELISA with immunoabsorbent-purified mycobacterial antigen for serodiagnosis of tuberculosis. 250 85

The chemotactic activity of elastin-derived peptides (EP) for human polymorphonuclear leukocytes (PMNL) was investigated using the under agarose method. The EP were produced by digesting the bovine ligament elastin with porcine pancreatic elastase. Thus prepared digest had weak chemotactic activity for PMNL. The mean chemotactic index for all tested EP concentrations did not exceed 1.30 and was lower than that obtained with zymosan-activated serum (ZAS, n-formyl-methionyl-leucyl-phenylalanine (FMLP) 2.2 +/- 0.40, 3.1 +/- 0.32, (n = 10) respectively. However, EP (50 micrograms) after injection to the mouse pleural cavity induced PMNL influx. The mean PMNL number found in this cavity was 0.09 +/- 0.03 x 10(6) for PBS and 0.18 +/- 0.03 +/- 10(6) for EP injection (p less than 0.01 n = 6). Human PMNL during 60 min incubation with EP (1 to 10 micrograms/ml) or with EP and cytochalasin B (CB 4.8 micrograms/ml) released myeloperoxidase and low amounts of hydrogen peroxide. At 1 micrograms/ml and in presence of CB elastin digest was nearly as active in myeloperoxidase release as FMLP (300 ng/ml). The values reached 17.1 +/- 2.5 and 19.7 +/- 2.1% of the total activity of whole cell lysate, respectively. The obtained results suggest that EP produced in vivo in the site of inflammation could modulate to some extent its course by enhancing PMNL influx and their activation. It seems that such mechanism of enhancement of the inflammatory response may occur in the lungs which are rich in elastin fibers.
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PMID:Chemotactic activity of elastin-derived peptides for human polymorphonuclear leukocytes and their effect on hydrogen peroxide and myeloperoxidase release. 256 30

The specific and saturable binding of FITC conjugate of aggregated goat IgG to goat peripheral blood lymphocytes was studied in PBS containing 1% BSA. The polar nature of the specific interaction of heterologous aggregated IgG, IgG monomer and its fragment F(ab'2) with the cells was studied by ELISA using the peroxidase conjugated F(ab'2) of anti-human IgG under different conditions of pH and ionic strength.
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PMID:Binding of immunoglobulin G to peripheral blood lymphocytes. 297 35

Conditions of the enzyme immunoassay for the detection of HSV-I by the "sandwich"-method at all stages of the testing were optimized using monoclonal antibodies (monoAB). When identical concentrations of monoclonal antibodies and durations of their adsorption on polystyrene plates were used, the signal in EIA (A405) with carbonate buffer was by 30% higher than that for PBS. A similar increase in the signal was observed at a temperature of incubation of 37 degrees C as compared with that at 4 degrees C. Even during 18-hour incubation at 37 degrees C no inactivation of monoAB occurred. It was further shown that saturation of the surface of wells with protein was achieved at a concentration of monoAB 5-10 micrograms/ml, and under these conditions the optimal dilution of the conjugate was that corresponding to antibody concentration of 1.5 micrograms/ml. When ABDC peroxidase and 5-aminosalycilic acid were used as the substrate, the presence of HSV-I was regularly detected even with a concentrated virus preparation diluted 500-1000-fold (corresponding to approximately 5.0 1g TCID50).
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PMID:[Development of an immunoenzyme test for determining herpes simplex type 1 virus using monoclonal antibodies]. 303 3

The protein B of group B streptococci can bind in a nonimmune reaction to Ig of the IgG and IgM classes of various mammalian species (i.e., human, mouse, rabbit, and bovine). Protein B binding involves the Fc parts of both IgG and IgM molecules. Monoclonal or polyclonal IgG or IgM and the IgM-FC5 mu fragment of human myeloma protein combined with the protein B thereby inhibiting protein B-induced hemolysis in the CAMP reaction. The protein B/Ig complex can be dissociated with 1% Triton or guanidine-HCl (6 M). Mice infected intraperitoneally with sublethal doses of group B streptococci (GBS) and that received seven repeated intravenous injections of highly purified protein B during the first 9 h of infection developed fatal septicemia within 24 h with colony counts of up to 10(8) CFU/ml in the blood. Animals treated in the same way with either PBS or trypsinized protein B recovered. The protein B itself was not pathogenic when injected into healthy mice. Tissue sections of liver or spleen from mice infected with a lethal dose of GBS revealed the presence of protein B together with large numbers of cocci when stained by the peroxidase method using specific antibodies raised against purified protein B in the rabbit.
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PMID:Unspecific binding of group B streptococcal cocytolysin (CAMP factor) to immunoglobulins and its possible role in pathogenicity. 354 80

Using a monospecific, monoclonal antibody against the glucocorticoid receptor (GR), an immunocytochemical study was performed to investigate the intracellular localization of GR both in the presence or absence of ligand. With all fixation methods tested (paraformaldehyde, acetic acid in ethanol, Bouin's fixative, and bensochinone in PBS), it was possible to obtain specific GR staining. Fixation with paraformaldehyde was chosen for further studies on the effect of permeabilization, using several concentrations of Triton X-100 or saponin. A rat Rueber hepatoma (H-4-II-E) and a human uterus carcinoma (NHIK 3025) cell line were used as well as cultured hepatocytes from normal rat. The accessibility of the different cell compartments after fixation and permeabilization was tested for by using antibodies against cellular constituents with known locations (i.e. core-nucleosome proteins and tubulin), in combination with the anti-GR antibody in double immunofluorescence staining experiments. The specific GR stain obtained with the indirect peroxidase antiperoxidase technique or with fluorescein isothiocyanate-labeled second antibodies was shown to be present both in the cytoplasm and in the nucleus. Staining of all cellular compartments was abolished (peroxidase antiperoxidase) or diminished (fluorescein isothiocyanate) if the monoclonal antibody was preincubated with a 90% pure GR preparation. These findings are in contrast to recently reported immunocytochemical studies, where a strict nuclear existence of the estrogen and progestin receptors has been reported. Consequently, generalizations with regard to steroid receptor localization cannot be made. Furthermore, an in vitro model is described, where the effect of dexamethasone administration upon the localization of receptor staining in H-4-II-E cells can be studied.
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PMID:Intracellular localization of the glucocorticoid receptor: evidence for cytoplasmic and nuclear localization. 354 55

Insulin-like growth factor I (IGF-I) is present in multiple tissues and cell types. Expression of the IGF-I gene was examined in GH3 cells, a rat pituitary tumor cell line secreting GH and PRL. Increasing concentrations of RNA extracts of GH3 cells yielded a linear increase in hybridization intensity with a 32P-labeled mouse IGF-I cDNA probe. Northern analysis of GH3 cells poly(A) RNA revealed IGF-I mRNA transcripts 1.3, 5.3, and 7.7 kilobases in size. Poly(A) RNA extracts of BALBc/3T3 fibroblasts, a cell line dependent on exogenous somatomedins for DNA synthesis, and of JEG-3 cells, a choriocarcinoma cell line, did not hybridize with the IGF-I cDNA probe. GH3 cells showed positive immunoperoxidase staining using a rabbit anti[Thr59]IGF-I antibody which was largely blocked by prior incubation of the antibody with excess IGF-I. Negligible background peroxidase activity was present in cells incubated with a rabbit nonimmune serum and PBS. Furthermore, BALBc/3T3 fibroblasts showed only weak specific staining with the IGF-I antibody. Finally, GH3 cells secreted IGF-I into the culture medium in a time-dependent fashion, while neither 3T3 nor JEG-3 cells produced detectable medium levels of the peptide after 72 h of incubation. As IGF-I is known to inhibit GH production by the pituitary, the data shown suggest that locally produced IGF-I may regulate GH secretion in an autocrine or paracrine fashion.
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PMID:Insulin-like growth factor I gene expression in GH3 rat pituitary cells: messenger ribonucleic acid content, immunocytochemistry, and secretion. 355 29

The morphological localization of antigen B (AgB) in the tissues of the Taenia solium metacestode was studied by immunological and biochemical methods. Indirect immunofluorescence carried out on vibratome sections showed that AgB is widely distributed throughout the tissue. A more intense fluorescence was observed in the tegumentary cytons of the bladder wall and in the lumen of the spiral canal of the invaginated scolex. Ultrastructural analysis of larvae washed in PBS after dissection from meat and then incubated with rabbit antibodies against AgB, followed by peroxidase-labeled goat anti-rabbit IgG, did not exhibit electron-dense material on the external surface. Larvae fixed in glutaraldehyde immediately after dissection and exposed to the immunoperoxidase reagents did exhibit electron-dense material on microtriches, indicating that AgB is only loosely bound to the external surface. Crude extracts of surface-radioiodinated cysticerci analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) contained no labeled proteins with the molecular weight of AgB. Autoradiography of the immunoelectrophoretograms in which the crude extract was confronted with antibodies to AgB demonstrated that this antigen was not labeled, and therefore is not exposed on the tegumentary surface. The results suggest that AgB is synthesized by the tegumentary cytons of the parasite and secreted through the tegumental membrane into the host tissues and the lumen of the spiral canal.
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PMID:Histological and ultrastructural localization of antigen B in the metacestode of Taenia solium. 355 14

The antigenicity and specificity of crude antigens collected during the in vitro maintenance of Taenia hydatigena and T. ovis, excretory/secretory (ES) antigens, were assessed in a peroxidase microenzyme-linked immunosorbent assay (ELISA), using sera from lambs given experimental monospecific infections with T. hydatigena, T. ovis, Echinococcus granulosus or Fasciola hepatica. ES antigens of larval cysts of T. ovis and T. hydatigena were less reactive than those of adult or oncosphere stages. Strong interspecific cros-reactions occurred between all antigen preparations, and these antigens offered no better specificity than crude somatic extracts. IgG1 was the major immunoglobulin detected in sera from lambs experimentally infected with T. ovis or T. hydatigena using antigens prepared from sonicated oncospheres. Discrete peaks of anti-oncospheral antibodies were detected following initial and challenge infections with eggs (whether the homologous or heterologous species), when sera were assayed with a PBS sonicate or an ES antigen from oncospheres. However, when oncospheres solubilised with sodium deoxycholate were used, the antibody response was prolonged and resembled that reported previously when somatic extracts of adult and metacestode stages were used as antigen. The results showed that oncospheres share antigens in common with other life-cycle stages, but also support the notion that they may possess some unique stage-specific antigenic determinants.
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PMID:Antibody responses of experimentally infected lambs to antigens collected during in vitro maintenance of the adult, metacestode or oncosphere stages of Taenia hydatigena and Taenia ovis with further observations on anti-oncospheral antibodies. 618 May 65

We examined the localization of five pregnancy-associated proteins such as pregnancy specific beta 1-glycoprotein (SP1), human chorionic gonadotropin (HCG), human placental lactogen (HPL), alpha 2-PA-glycoprotein (SP3) and pregnancy-associated plasma protein-A (PAPP-A) in the placentae of early and term pregnancies by means of the PAP method in immunohistochemical technology. It was found that the degree of staining of these proteins did not reflect their concentration in serum at each gestational age. Therefore, the concentrations of these proteins in the solution extracted from the placenta were measured. 1) Placental tissues were fixed with a 10% neutral formaldehyde solution and these were embedded into paraffin blocks. These specimens were used for the PAP method. The localizations of five pregnancy-associated proteins from 10 placentae at the gestational age of 7 to 10 weeks were compared with those at the gestation age of 38 to 41 weeks from 7 patients. The staining degree of SP1 in free villi was pale in both early and term pregnancies. HCG was stained deeply in early pregnancy but pale at term pregnancy. HPL was stained deeply at both gestational ages. Horseradish peroxidase reaction products from SP1, HCG and HPL were located chiefly in the syncytiotrophoblast. SP3 was not stained on the placental tissue. PAPP-A was stained to a greater extent in the cytotrophoblast in early pregnancy but pale in the syncytiotrophoblast at term pregnancy. 2) The concentrations of SP1, HCG, HPL, SP3 and PAPP-A were measured in the placental tissues in both early and term pregnancies. Placental tissues were obtained from 24 normal pregnancy patients aborted artificially at 8 to 11 weeks gestation and from 28 patients terminated by normal deliveries at 38 to 40 weeks gestation. The tissue was homogenated with 3 volumes of 1/2 PBS (0.005M phosphate-buffered 0.07M sodium chloride, pH 7.4). The supernatant was removed after centrifugation and stored at -20 degrees C until assayed. The concentration of SP1 was measured by single radial immunodiffusion. That of HCG was assayed by a directed Latex agglutination test (Gestate Slide Eiken). The concentrations of HPL, SP3 and PAPP-A were quantified by rocket immunoelectrophoresis. No significant difference in SP1 levels was shown between early and term pregnancies, and the SP1 level was 4.3 +/- 1.3 (mean +/- 1 S.D.) mg/dl at term pregnancy. The HCG level was 1,100 +/- 300 IU/ml in early pregnancy and at least 20-fold higher than that at term pregnancy.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:[Placental tissue concentration of pregnancy-associated proteins in early and term pregnancies]. 619 24


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