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  • 1
    Electronic Resource
    Electronic Resource
    TROPHOBLASTIC TUMOUR, ORAL CONTRACEPTIVE THERAPY AND PREGNANCY ASSOCIATED ALPHA2-GLYCOPROTEIN (PAAG), CASE REPORT (1977)
    Oxford, UK : Blackwell Publishing Ltd
    BJOG 84 (1977), S. 0 
    Details
    ISSN: 1471-0528
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Pregnancy associated alpha2-glycoprotein (PAAG) and human chorionic gonadotrophin (HCG) levels were studied in a patient with an invasive mole who was being treated with cytotoxic drugs and oral contraceptives. Both the PAAG and HCG levels fell during cytotoxic drug treatment while oral contraceptives caused a rise in PAAG concentrations. A relation between oestrogen-induced PAAG and prolonged survival of trophoblastic tumour is proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-0528.1977.tb12667.x
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  • 2
    Electronic Resource
    Electronic Resource
    Increased Number of IgG Fc Receptors on Monocyte-Enriched Peripheral Blood Leucocytes from Patients with Rheumatoid Arthritis (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 16 (1982), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The number of free Fc receptors (FcR) per cell and the association constant (Kass) for the binding of monomeric IgG were determined for monocyte-enriched peripheral blood mononuclear cells, isolated from 16 patients with active classical rheumatoid arthritis (RA) and from 15 normal healthy donors. The assay system was based on binding under equili brium conditions of 125I-labelled monomeric rabbit IgG to monocytes purified from peripheral blood on a continuous gradient of Petcoll. Monocytes from 14 untreated RA patients (6 seropositive, 8 seronegative) expressed on the average 4.8±1.3 × 104 FcR/cell. This number was significantly higher (P〈0.01) than that found in the control group (3.46±0.7 × 104 FcR/cell). There was also a significant difference between the mean Kass of the RA group and the control group-2.1±0.7 × 1031/mol and 2.6±1.0 × 103 1/mol, respectively (0.05 〉P〉 0.01). Two seropositive RA patients receiving systemic treatment with penicillamine expressed the same number of FcR/cell as the mean of the control group (3.6 ± 104). Levels of circulating immune complexes (CIC) and of the complement-factor C3 split product C3d were also measured. No correlation was found between the number of FcR/cell and the concentration of C3d, but there was a weak correlation between the number of FcR/ccll and the level of CIC.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1982.tb00724.x
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  • 3
    Electronic Resource
    Electronic Resource
    β2-Microglobulin-containing IgG Complexes in Sera and Synovial Fluids of Rheumatoid Arthritis and Systemic Lupus Erythematosus Patients (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 13 (1981), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The occurrence and composition of complexed β2-microglobulin (β2m) In sera and synovial fluids of rheumatoid arthritis and systemic lupus erythematosus patients and control persons was investigated. β2m-containing complexes were detected In immune complex (IC)-enriched fractions isolated by precipitation with 3% polyethylene glycol 6000, In the macromolecular peaks after Sephadex G-200 gel filtration, and in IC desorbed from solid-phase Clq. β2m complexes were demonstrated also after precipitation of redissolved PEG-insoluble material by anti-human β2m serum or isolation of the complexes by use of Sephadex-anti-β2m. IgG was co-isolated with with β2m on Sephadex-anti-β2m, and free β2m inhibited the binding of IgG to Sephadex anti-β2m, Indicating that IgG was present in the complexed β2m. Analysis by SDS–polyacrylamide gradient electrophoresis under reducing conditions indicated that the purified β2m complexes contained IgG and β2m.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1981.tb00107.x
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation and Characterization of Porcine Mannan-Binding Proteins of Different Size and Ultrastructure (1996)
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 43 (1996), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The authors report on the purification and characterization of mannan-binding proteins (MBP) isolated from porcine serum. The MBPs were purified by use of PEG precipitation, affinity chromatography on mannan-Sepharose, protein A- and anti-porcine IgM-Sepharose followed by gel filtration. The MBP proteins were collagenase sensitive and showed γ1-γ2-electrophoretic mobility. The MBP designated pMBP-28 had a molecular mass of 28 kDa when analysed on SDS-PAGE under reducing conditions and eluted corresponding to a molecular mass of approximately 700 kDa on gel filtration chromatography. Electron micrographs of pMBP-28 revealed an oligomeric protein similar to rodent MBP-A and human MBP but with a predominance of penta- and hexameric molecules. Another protein designated pMBP-27 was composed of peptides of 27 kDa and had an Mr of 300–350 kDa on gel filtration chromatography. Electron microscopy of pMBP-27 showed dimer and trimer molecules; the trimers without distinct stalk regions. The N-terminal 26 (pMBP-27) and 24 (MBP-28) amino acid residues showed 54% and 58% identity with human MBP. pMBP-28 showed a higher degree of sequence similarity to rat and mouse MBP-A (60% identity) than to mouse and rat MBP-C (41–45% identity). Both pMBPs exhibited Ca2+-dependent binding to D-mannose immobilized on agarose but no significant binding to N-acetyl-D-glucosamine- or fucose-agarose. The results further suggested the presence of a third pMBP which copurified with pMBP-27 but this protein was not sequenced.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.1996.d01-39.x
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  • 5
    Electronic Resource
    Electronic Resource
    Detection of IgG Aggregates or Immune Complexes Using Solid-Phase C1q and Protein A-Rich Staphylococcus aureus as an Indicator System (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 4 (1975), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A radioimmunoassay for detection of Clq-binding IgG aggregates and antigen-IgG antibody complexes is described The assay makes use of solid-phase Clq and 32p-labelled protein A-rich Stphylococcusaureus as an indicator system. Both 19S and heavier IgG aggregates that fixed Clq were detected The sensitivity of the assay permitted detection of heavy (19–25S) IgG aggregates at a concentration of 8 μg/ml or less. The results indicated that detection of IgG in this assay is dependent on the degree of IgG polymerization and the molar ratio between the solid-phase Clq and the IgG polymers. Albumin-anti-albumin complexes, preformed at equilibrium with antibody to antigen molar ratios of 2:1 to 3:1 and at antigen concentrations of 25 to 40 μg/ml. were also detectable using the described radioimmunoassay
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1975.tb02675.x
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  • 6
    Electronic Resource
    Electronic Resource
    The Influence of C3-Coated Homologous Erythrocytes on Pokeweed-Mitogen-Induced Polyclonal Differentiation of Human B Cells (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 30 (1989), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The present study was undertaken in order to test the hypothesis that homologous erythrocytes (E) coated in vivo with C3d could modulate the immunoglobulin (Ig) synthesis of human peripheral blood mononuclear cells (PBMC), stimulated with pokeweed mitogen (PWM) in vitro. E from healthy individuals were found to enhance markedly the Ig synthesis of PBMC cultures stimulated with suboptimal doses (0.01 μg/ml) of PWM. E coated in vivo with increasing amounts of C3d (1.4–6.3 times the amounts on normal E), obtained from patients with systemic lupus erythematosus, failed to induce any significant increase in Ig synthesis of PBMC cultures stimulated with suboptimal PWM doses, compared with cultures co-stimulated in parallel with normal E. In contrast, an increase in IgM and IgG synthesis was observed in about 50% of PBMC cultures from different donors when stimulated with PWM in the presence of L- touted with Ohm vivo (from a patient with congenital factor I deficiency), compared with the Ig synthesis in cultures co-stimulated in parallel with normal E. In contrast to the inability of C3d-coated E to modulate B-cell proliferation, the monoclonal anti-CR2 antibody OKB7 was found to be mitogenic for unstimulated peripheral B cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1989.tb01203.x
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  • 7
    Electronic Resource
    Electronic Resource
    A Monoclonal IgG Protein with Antibody-Like Activity for Transferrin and with X Chains of an Unusual Molecular Size (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 3 (1974), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The serum of a patient with high serum iron and transferrin levels contained an abnormal brownish protein with a sedimentation coefficient of 9.9S. At pH 3.5 this protein dissociated, and on gel filtration it proved to be a complex of one molecule of monoclonal IgGI and two molecules of transferrin. At pH 7.6 the isolated 59Fe-labeled transferrin recombined with most of the separated IgGI, forming again the original complex. Of particular interest was that the polypeptide kappa chains of this IgG seemed to have a molecular size of 27,000 to 28,000 daltons. We came to the conclusion that the serum of this patient contained a monoclonal protein with antibody-like specificity for normal transferrin. Transferin only circulated as a complex with this protein at high levels in the serum and probably accumulated in the liver, giving use to severe hemosiderosis and cirrhosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1974.tb01324.x
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  • 8
    Electronic Resource
    Electronic Resource
    Cell-Mediated Immunity in Guinea Pig and Man to a Salmonella typhi Glycoprotein Complex Assessed by Migration Inhibition Methods (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 3 (1974), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A Salmonella typhi glycoprotein preparation in concentrations of 5 to 10 μg/ml strongly inhibited the migration of peritoneal exudate cells (PEC), obtained from guinea pigs immunized with S. typhi vaccine in Freund's complete adjuvant (FCA) PEC from animals injected with saline in FCA were also inhibited but to a lesser extent, whereas cells from guinea pigs that had received only S. typhi vaccine or normal guinea pigs showed variable and weaker inhibition. PEC from all guinea pigs receiving FCA were strongly inhibited by 5 to 15 μg PPD/ml. These PPD concentrations had no inhibitory effect on exudate cells from guinea pigs receiving S. typhi vaccine only. The S.typhi glycoprotein concentration (5 and 10 μg/ml) primarily used in the migration inhibition studies had negligible inhibitory effect on the phytohemagglutinin (PHA)-induced DNA, RNA, and protein syntheses in guinea pig lymph node cells. In the human system only blood leukocytes of donors who had received their third or fourth booster of heat-killed S. typhi vaccine within the latest 2 years were inhibited in their in vitro migration by the S. typhi glycoprotein complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1974.tb01294.x
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  • 9
    Electronic Resource
    Electronic Resource
    Characterization of a Lectin in Human Plasma Analogous to Bovine Conglutinin (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 26 (1987), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The structural characteristics of a human plasma protein analogous to bovine conglutinin were studied. The protein was previously found to bind to complement-reacted IgG in a calcium-dependent and N-acetyl-D-glucosamine-inhibitable manner and it further shows cross-reactivity with anti-bovine conglutinin antibody. By gel permeation chromatography the conglutinin activity in human plasma was localized to fractions containing proteins of Mj at around 700,000. The conglutinin was localized by one ELISA for antigen determinants and by another for biological activity. When analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions these fractions were shown to contain proteins of about 300,000. When human conglutinin-like protein, partially purified by affinity chromatography, was analysed unreduced by SDS-PAGE followed by western blotting, the cross-reacting anti-bovine conglutinin antibody bound to a protein with an Mr of 330,000. When the sample was reduced and alkylated before electrophoresis a band of 66,000 was immunostained. The 330,000 and 66,000 proteins were shown to be collagenase sensitive. 125I-iC3b was seen to bind to the 330,000 band when incubated with western blots of partially purified human conglutinin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1987.tb02279.x
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  • 10
    Electronic Resource
    Electronic Resource
    Demonstration in Human Plasma of a Lectin Activity Analogous to that of Bovine Conglutinin (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 26 (1987), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Evidence of the existence in human plasma of an activity analogous to that of bovine conglutinin is presented. The human plasma component was characterized antigenically and functionally. Human plasma was shown to agglutinate complement-coated erythrocytes in the presence of Ca2+, and this conglutination was inhibited by EDTA. The molecule also binds to complement-reacted solid phase IgG and to zymosan in the presence of Ca2+. The binding to complement is not inhibited by N-acetyl-D-mannosamine, but is inhibited by N-acetyl-D-glucosamine, as previously shown for bovine conglutinin. Antibodies raised against bovine conglutinin cross-react with the human protein. The plasma concentration of the conglutinin-like protein showed a high inter-individual variation between apparently healthy donors. Unlike bovine conglutinin, the human conglutinin activity could not be demonstrated in serum but only in plasma. The activity was more stable in plasma containing metal-ion chelators like EDTA and citrate than in heparin or hirudin plasma.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1987.tb02267.x
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