Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • 1975-1979  (6)
Source
Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    The Disappearance of SpA-IgG Antibody Complex on ‘Armed’ Lymphoid and Macrophages Cells (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 7 (1978), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The disappearance rate of rabbit IgG antibody complexed with protein A from Staphylococcus aureus (SpA) on ‘armed’ mouse and rabbit spleen lymphocytes, and on ‘armed’ mouse peritoneal macrophages, was investigated by rosette and antibody-dependent cellular cytotoxicity (ADCC) assays. The half time of disappearance of complex from the surface of lymphoid cells was found to be 36 min in both assays. Macrophages, ‘armed’ with IgG antibody complexed with SpA, bind the corresponding antigens and subsequently lyse the target cells by extracellular and/or intracellular mechanisms. ‘Armed’ macrophages have both ADCC and phagocytosis ability, although a short half-time of disappearance of complex was observed (8 min).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1978.tb00463.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Arming of Lymphoid Cells by IgG Antibodies Treated with Protein A from Staphylococcus aureus (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Mouse spleen lymphocytes treated with rabbit IgG anti-sheep erythrocytes (SRBC) complexed with protein A of Stapbylococcus aureus (SpA) form rosettes with SRBC. The attachment of SRBC to lymphocytes was due to the binding of the SpA-IgG antibody complex to the surface of the lymphocytes and was thus considered ‘arming’ of the cells. Normal mouse spleen cells ‘armed’ with SpA-rabbit IgG anti-chicken erythrocytes (CRBC) kill specifically 51Cr-labeled CRBC ‘in vitro’ in the absence of free antibodies. The killing by these ‘armed’ cells is an effect of the cell-bound SpA-IgG antibody complex. Both the SRBC rosette formation and the cell-mediated CRBC killing was dependent on the concentration of the SpA-IgG antibody complexes used for ‘arming’ the cell. A 100-fold increase in rosette formation or in killing of target cells was recorded for lymphocytes treated with SpA-IgG antibody complexes in comparison with cell treated with noncomplexed IgG antibodies. The specific binding of SpA-IgG antibody complexes to the Fc receptors of mouse spleen cells was demonstrated by inhibition studies. More than 60% inhibition of the rosette formation and in the killing of target cells was shown for cell treated With normal rabbit IgG or its Fc fragment before addition of the SpA-IgG antibody complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb00262.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    A Method for the Detection and Quantitation of Fc Receptor Sites on Cells (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A new rosette technique for identification of Fc-receptor-bearing cells is based on the ability of sheep erythrocyte coated with protein A of Staphylococcus aureus (ES) to form rosettes with cell treated with monomeric IgG or aggregated IgG. The IgG is attached to lymphocytes through its Fc region and to a trypsin-resistant but pronase sensitive receptor (considered an Fc receptor) The ES rosette technique facilitates studies of the interaction of IgG with Fc receptor sites; the binding of any IgG preparation reacting with protein A of Staphylococcus aureus (SpA) can be studied by the technique. Inhibition of rosette formation by SpA was used for quantitation of IgG fixed to the cell surface (that is, the number of Fc reception/cell). The sensitivity of the method permits quantitation of less than 105 IgG molecules bound to the Fc receptors. The relative affinity constant between Fc receptors and IgG ligands was estimated by plotting the percentage of ES rosettes as a function of IgG concentration and calculating the reciprocal of the IgG concentration giving half the maximal number of ES rosettes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb00263.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Cell Separation by Staphylococcal Protein A-Coated Erythrocytes (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 method for cell separation according to cell surface markers is described. Heat-aggregated human IgG or IgG antibodies, raised to surface markers of mouse lymphocytes–for example, Ig or theta antigen–are allowed to react with the lymphocytes. When these cells are incubated with sheep erythrocytes coated with protein A of Staphylococcus aureus, rosettes are formed. These rosettes can be separated from nonrosetted lymphocytes by density gradient centrifugation. The erythrocytes of the rosettes are disrupted by complement action or by osmotic shock, and the lymphocytes are recovered. Immunoglobulin-protein A complexes are shed off the cell surfaces by cultivation. In this way cells with, as well as those without, surface markers could be obtained with high purity (up to 80%) and with high viability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1975.tb02652.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Receptors for polymerized albumin on liver cells (1977)
    Springer
    Cellular and molecular life sciences 33 (1977), S. 1046-1047 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary By the use of rabbit polymerized albumin labelled with fluorescein isothiocyanate, or coated on sheep red blood cells, specific receptors on rabbit liver cells were demonstrated. The possible biological role of these receptors is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01945961
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Binding of cytophilic rabbit IgG to homologous hepatocytes (1979)
    Springer
    Cellular and molecular life sciences 35 (1979), S. 763-765 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Rabbit liver cells were able to bind cytophilic monomeric and polymeric homologous IgG via their Fc receptor binding sites (FcR). On the other hand, non-cytophilic rabbit IgG did not bind to hepatocytes, even after its aggregation. The present findings suggest that FcR on rabbit liver cells are specific for cytophilic monomeric IgG but do not significantly bind non-cytophilic, polymeric IgG.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01968232
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...