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  • 1
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  Jahrestagung der Gesellschaft für Medizinische Ausbildung - GMA; 20081002-20081005; Greifswald; DOC08gma5 /20080819/
    Publication Date: 2008-08-20
    Keywords: ddc: 610
    Language: German
    Type: conferenceObject
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  • 2
    Keywords: RECEPTOR ; CELLS ; ENDOTHELIAL-CELLS ; CELL ; Germany ; human ; PROTEIN ; PROTEINS ; DRUG ; cell line ; LINES ; FAMILY ; tumour ; BINDING ; CELL-LINES ; MEMBER ; MEMBERS ; antibodies ; antibody ; TARGET ; IDENTIFICATION ; PLASMA ; Western-blot ; MEMBRANE ; SPECTROMETRY ; CELL-LINE ; LINE ; PURIFICATION ; SURFACE ; isolation ; AFFINITY ; ARGININE METHYLATION ; BRUSH-BORDER ; CONFORMATIONALLY MODIFIED ALBUMINS ; LUNG-CANCER DETECTION ; METHOTREXATE-ALBUMIN ; TREATED SERUM-ALBUMIN ; CALRETICULIN ; albumin-binding proteins (ABPs) ; heterogeneous nuclear ribonucleoproteins (hnRNP) ; crossl
    Abstract: Since albumin is being developed as a drug carrier to target tumours the search for albumin-binding proteins (ABPs), which play a role in cell surface binding and endocytosis of native and conjugated albumins becomes more and more interesting. We isolated five different proteins from purified plasma membranes from three different human tumour cell lines (CCRF-CEM, MV3 and MCF7) by albumin affinity chromatography and identified them as four members of the heterogeneous nuclear ribonucleoproteins (hnRNP) family and calreticulin by matrix-assisted laser desorption ionisation time-of-flight mass spectrometry. Contamination of the plasma membrane preparation by nuclear membranes was excluded with anti-nucleopore antibodies. Western blot analyses of plasma membranes showed ABPs with the same molecular weights as the albumin-affinity isolates. Tryptic digestion of intact cells was used to determine the sidedness of the albumin-binding property, which is oriented to the exterior of the cell. Localisation to the plasma membrane and albumin binding is a novel property of hnRNP. (C) 2003 Elsevier Inc. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 14757165
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  • 3
    ISSN: 1432-2021
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Abstract The cation distribution in the synthetic samples of olivine-type structure with composition (Fe x Mn1−x )2SiO4 was determined at room temperature and confirms previous Mössbauer results. At low temperature an antiferromagnetic ordering is observed. The magnetic structures can be described in the crystallographic cell (i.e. k=0). They are interpreted on the basis of the irreducible representations (modes) of the symmetry groups which are compatible with Pnma. The dominant modes observed for all compounds, including Fe2SiO4 and Mn2SiO4, only differ in their direction. The main direction of magnetization is dominated by the Fe2+ single-ion anisotropy. At 4.2K, for x=0.29, it is parallel to the c-axis, whereas for x=0.76 the direction is parallel to the b-axis. The anisotropy of the M1-sites dominates in the first case, whereas M2-anisotropy dominates in the second case. The influence of temperature is demonstrated for x=0.50 where c is the main direction at 4.2K, when it is b at 38K.
    Type of Medium: Electronic Resource
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