Zobrazeno 1 - 10
of 234
pro vyhledávání: '"S.‐E. Svehag"'
Autor:
D. Burger, S.-E. Svehag
Publikováno v:
Acta Pathologica Microbiologica Scandinavica Section C Immunology. :45-52
The applicability of affinity chromatography to the isolation of Clq-binding immune complexes (IC) in sera was explored. Purified human Clq was covalently coupled to agarose or adsorbed to IgG-agarose resins. Sera containing preformed virus-antibody
Publikováno v:
Scandinavian Journal of Immunology. 46:331-337
Serum amyloid P component (SAP) is a member of the phylogenetically conserved and structurally related group of proteins called pentraxins. SAP exhibits multispecific calcium-dependent binding to oligosaccharides with terminal N-acetyl-galactosamine,
Autor:
Uffe Holmskov, Ove Andersen, P. Storgaard, E. Skriver, Peter Højrup, E. Holm Nielsen, H. Mortensen, S.-E. Svehag, G. Leslie
Publikováno v:
Scandinavian Journal of Immunology. 43:289-296
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 Ig
Publikováno v:
Scandinavian Journal of Immunology. 42:373-380
We report that alpha-2-macroglobulin (alpha 2M) can form complexes with a high molecular weight porcine mannan-binding protein (pMBP-28). The alpha 2M/pMBP-28 complexes was isolated by PEG-precipitation and affinity chromatography on mannan-Sepharose
Autor:
Peter Junker, R. G. Q. Leslie, Anders Jørgen Svendsen, S E Svehag, J M Rasmussen, Claus Henrik Nielsen, H. V. Marquart
Publikováno v:
Marquart, H V, Svendsen, A J, Rasmussen, J M, Nielsen, C H, Junker, P, Svehag, S E & Leslie, R G 1995, ' Complement receptor expression and activation of the complement cascade on B lymphocytes from patients with systemic lupus erythematosus (SLE) ', Clinical and Experimental Immunology, vol. 101, no. 1, pp. 60-65 . https://doi.org/10.1111/j.1365-2249.1995.tb02277.x
It has previously been reported that the expression of the complement receptors, CR1 on erythrocytes and blood leucocytes and CR2 on B cells, is reduced in patients with SLE, and that the reduced expression of CR1 on erythrocytes is related to diseas
Publikováno v:
The Journal of Immunology. 153:307-315
Human cells infected with certain viruses acquire the ability to activate the alternative pathway (AP) of complement. Complement receptor 2 on EBV-infected lymphoblastoid cell lines has been reported to act as the covalent binding site for C3b during
Publikováno v:
Scandinavian Journal of Immunology. 33:81-88
The highly glycosylated envelope glycoprotein (gp 160) of human immunodeficiency virus (HIV) interacts with the CD4 molecule present on the membrane of CD4+ cells and is involved in the pathobiology of HIV infection. Lectins bind glycoproteins throug
Autor:
Hans Henrik Jepsen, S.‐E. Svehag, Lene Jarlbæk, Henrik Isager, Børge Teisner, Lise SchrØDer, J M Rasmussen, Uffe Holmskov
Publikováno v:
APMIS. 98:637-644
Erythrocytes (E) from a cross-sectional group of 22 outpatients with systemic lupus erythematosus (SLE) and/or mixed connective tissue disease (MCTD), the majority without active disease (n = 14), were analyzed for CR1 antigen expression and capacity
Autor:
Susanne Boysen, Peter Højrup, S.-E. Svehag, Per Wittenhagen, Jens Jørgen Lønsmann Iversen, Ellen Holm Nielsen, Inger Andersen, Berit Fogh-Schultz
Publikováno v:
Boysen, S, Fogh-Schultz, B, Andersen, I, Højrup, P, Iversen, J J L, Wittenhagen, P, Nielsen, E H & Svehag, S-E 2004, ' Recombinant human serum amyloid P component from Pichia pastoris: Production and characterization. ', Protein Expression and Purification, vol. 35, pp. 284-292 . https://doi.org/10.1016/j.pep.2004.01.011
Human serum amyloid P component (SAP) was expressed in the methylotrophic yeast Pichia pastoris . SAP cDNA was placed under control of regulatory sequences derived from the alcohol oxidase gene (AOX1), and its protein product was secreted using the S
Publikováno v:
Journal of clinical immunology. 20(6)
Serum amyloid P component (SAP) binds in vitro to DNA; based on findings in SAP-deficient mice it was proposed that SAP's role is to handle chromatin and DNA, thereby preventing formation of anti-DNA antibodies. For the first time we have shown the p