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Polyclonal B-cell activation by a synthetic analogue of bacterial lipoprotein is functionally different from activation by bacterial lipopolysaccharide

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dc.creator Martínez-Alonso, Carlos
dc.creator Kleine, B.
dc.creator Sprenger, R.
dc.creator Bessler, W. G
dc.date 2008-02-06T11:26:35Z
dc.date 2008-02-06T11:26:35Z
dc.date 1987-05
dc.date.accessioned 2017-01-31T00:59:57Z
dc.date.available 2017-01-31T00:59:57Z
dc.identifier Immunology 1987 May; 61(1): 29–34.
dc.identifier PMID: 3495485
dc.identifier http://hdl.handle.net/10261/2872
dc.identifier.uri http://dspace.mediu.edu.my:8181/xmlui/handle/10261/2872
dc.description The reactivity of 38 murine strains to a synthetic analogue of bacterial lipoprotein, tripalmitoyl-pentapeptide (TPP), was tested and compared with the reactivity to lipopolysaccharide (LPS). These strains include common laboratory mice and H-2 recombinant inbred lines, as well as some newly bred lines originating from animals recently captured in different regions of Europe. All animals analysed were reactive to TPP and polyclonally activated to proliferation and immunoglobulin synthesis. Large differences in mitogen reactivities of various H-2 recombinant inbred strains suggest that MHC or closely linked gene products influence the reactivity to the LPS and TPP mitogens. By analysing the frequencies of precursor cells reactive to TPP or LPS and the isotype patterns obtained after stimulation, we demonstrated that both mitogens activate individual B cells in different ways.
dc.description Peer reviewed
dc.format 997404 bytes
dc.format application/pdf
dc.language eng
dc.publisher British Society for Immunology
dc.rights openAccess
dc.title Polyclonal B-cell activation by a synthetic analogue of bacterial lipoprotein is functionally different from activation by bacterial lipopolysaccharide
dc.type Artículo


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