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  • 1
    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.
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  • 2
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Mouse mannan-binding protein (MBP) was identified in serum by its Ca2+ -dependent binding to mannan. On gel permeation chromatography, the protein eluted corresponding to a molecular weight of approximately 750 kDa. Analysed on SDS-PAGE under reducing conditions, the polypeptide showed an apparent molecular weight of 28 kDa, while several high molecular weight bands were seen under non-reducing conditions. The presence of collagen-like domains within the molecule was indicated by a high glycine content (14.9%) and substantiated by sensitivity to collagenase. Rabbit anti-mouse MBP antisera were raised. The concentration of MBP in serum from normal mice was measured by rocket immunoelectrophoresis and found to be from below 1 μg/ml to 100 μg/ml (average 50 μg/ml, n= 60). The binding of mouse MBP to mannan could be inhibited by mono- and disaccharides in the following order of potency: L-fucose 〉 D-mannose 〉 N-acetyl-D-glucosamine 〉 maltose 〉 D-mannoheptulose 〉 D-glucose 〉 N-acetyl-D-mannosamine ≫ lactose 〉 D-galactose ≫ N-acetyl-D-galactosamine. Mouse MBP was shown to activate the classical complement cascade after binding to mannan. The sequence of 14 NH2- terminal amino acid residues of the molecule showed 93% identity to rat MBP-A and complete identity to the translated cDNA sequences for mouse MBP-A and mouse Ra-reactive factor component P28b (RaRF P28b) published previously. The amino acid composition of mouse MBP showed a high degree of homology to MBPs from other species and mouse RaRF P28b.
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  • 3
    ISSN: 1439-6327
    Keywords: Capillary supply ; Immunohistochemical staining ; Anti-collagen type IV ; Histochemical staining Amylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract An immunohistochemical method, based on an indirect peroxidase method for staining of capillaries containing collagen type IV, is presented. Biopsies from the vastus lateralis muscle of eight endurance trained runners were stained and counted for capillaries with the collagen type IV method and with the widely used amylase-PAS method. The mean number ± SEM of capillaries per fibre was 2.48±0.09 with the collagen type IV method and 2.41±0.08 with the amylase method. The 95% confidence intervals for the differences between the two methods were −0.03 to 0.15. We conclude that the collagen type IV immunohistochemical method for capillary staining is comparable with the amylase method under optimum conditions, but that it is likely to be more dependable. It also has the advantage that it reveals fibre outlines.
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  • 4
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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