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  • 1
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    FEBS Letters 292 (1991), S. 128-132 
    ISSN: 0014-5793
    Schlagwort(e): Aldolase A ; CAT assay ; Gene expression ; Promoter ; Rat
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 2
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    FEBS Letters 292 (1991), S. 128-132 
    ISSN: 0014-5793
    Schlagwort(e): Aldolase A ; CAT assay ; Gene expression ; Promoter ; Rat
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 3
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 119 (1984), S. 575-581 
    ISSN: 0006-291X
    Schlagwort(e): [abr] 0.02% Ficoll; 0.02% polyvinylpyrrolidone ; [abr] 1x Denhardt; 0.02% bovine serum albumin ; [abr] DBM paper; diazobenzyloxymethyl paper ; [abr] NADH; nicotinamide adenine dinucleotide (reduced) ; [abr] NEPHGE; non-equilibrated pH gradient gel electrophoresis ; [abr] SDS; sodium dodecyl sulfate ; [abr] SSC; standard saline citrate ; [abr] cDNA; complementary DNA ; [abr] kb; kilobase ; [abr] oligo(dT) cellulose; oligodeoxythymidylate cellulose ; [abr] poly(A) RNA; polyadenylated RNA
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 4
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 119 (1984), S. 575-581 
    ISSN: 0006-291X
    Schlagwort(e): [abr] 0.02% Ficoll; 0.02% polyvinylpyrrolidone ; [abr] 1x Denhardt; 0.02% bovine serum albumin ; [abr] DBM paper; diazobenzyloxymethyl paper ; [abr] NADH; nicotinamide adenine dinucleotide (reduced) ; [abr] NEPHGE; non-equilibrated pH gradient gel electrophoresis ; [abr] SDS; sodium dodecyl sulfate ; [abr] SSC; standard saline citrate ; [abr] cDNA; complementary DNA ; [abr] kb; kilobase ; [abr] oligo(dT) cellulose; oligodeoxythymidylate cellulose ; [abr] poly(A) RNA; polyadenylated RNA
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 5
    Digitale Medien
    Digitale Medien
    Springer
    Clinical and experimental nephrology 4 (2000), S. 43-48 
    ISSN: 1437-7799
    Schlagwort(e): Key words Nucleosome ; Human GBM ; Amyloid P component ; Lupus nephritis
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Background. Tissue amyloid P component is a normal constituent of the human glomerular basement membrane (GBM) and is immunologically identical to the serum amyloid P component, a major DNA binding protein in serum. We postulate that DNA or nucleosome core particles could bind to human GBM via the amyloid P component. Methods. An immunofluorescence study was used to detect the amyloid P component of the GBM. An enzyme-linked immunosorbent assay system was used to test the binding capacity of calf thymus DNA and chicken erythrocyte nucleosome core particles to a preparation of human GBM. Results. Amyloid P component was detected along the capillary wall of the human glomerulus by immunofluorescence. DNA and nucleosome core particles bound to human GBM in a dose-dependent manner in the presence of Ca2+. Digestion of GBM with trypsin resulted in the reduction of binding of anti-serum amyloid P antibody, DNA, and nucleosome core particles to the GBM. Anti-serum amyloid P component (SAP) IgG blocked the binding of DNA and nucleosome core particles to the GBM. Conclusion. DNA and nucleosome core particles bind to the GBM through amyloid P components.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 6
    ISSN: 1432-2307
    Schlagwort(e): Tubular basement membrane ; Peritubular capillary ; Cationic antigen ; Ovalbumin ; Trinitrophenol
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract We developed an experimental protocol for planting exogenous antigens with different molecular weights and charges on the constituents of the renal tubulointerstitium. The cationized antigens were injected selectively into the left renal arteries of Wistar rats. Antigen localization was documented by immunohistochemistry on frozen sections. Cationized bovine serum albumin (BSA; 68 kDa, isoelectric point =9.5) localized almost exclusively along the glomerular capillary wall. After application of highly cationic polyethyleneimine, cationized BSA given subsequently was found in a linear distribution along the glomerular capillary wall and along the peritubular capillaries. The fate of highly cationized ovalbumin conjugated with trinitrophenol (TNP-OA), subjected to gel filtration to obtain monomers (42 kDa, isoelectric point 〉10) differed; it was deposited in a linear pattern on the tubular basement membrane (TBM) and Bowman's capsule, and remained up to 36 h after injection. Noncationized, monomeric TNP-OA (42 kDa, isolectnic point =4.6) showed fine granular deposition in the tubular epithelium exclusively. These findings indicate that the barrier of the glomerular BM acts selectively on antigens with different molecular weights. They either settle on the peritubular capillaries, after passing the glomerular, or reach the urinary space, after which they are reabsorbed by the tubular epithelial cells to reach the TBM.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 7
    ISSN: 1432-2307
    Schlagwort(e): Tubular basement membrane ; Peritubular capillary ; Cationic antigen ; Ovalbumin ; Trinitrophenol
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract We developed an experimental protocol for planting exogenous antigens with different molecular weights and charges on the constituents of the renal tubulointerstitium. The cationized antigens were injected selectively into the left renal arteries of Wistar rats. Antigen localization was documented by immunohistochemistry on frozen sections. Cationized bovine serum albumin (BSA; 68 kDa, isoelectric point =9.5) localized almost exclusively along the glomerular capillary wall. After application of highly cationic polyethyleneimine, cationized BSA given subsequently was found in a linear distribution along the glomerular capillary wall and along the peritubular capillaries. The fate of highly cationized ovalbumin conjugated with trinitrophenol (TNP-OA), subjected to gel filtration to obtain monomers (42 kDa, isoelectric point 〉10) differed; it was deposited in a linear pattern on the tubular basement membrane (TBM) and Bowman's capsule, and remained up to 36 h after injection. Noncationized, monomeric TNP-OA (42 kDa, isolectnic point =4.6) showed fine granular deposition in the tubular epithelium exclusively. These findings indicate that the barrier of the glomerular BM acts selectively on antigens with different molecular weights. They either settle on the peritubular capillaries, after passing the glomerular, or reach the urinary space, after which they are reabsorbed by the tubular epithelial cells to reach the TBM.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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