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Peptides eluted from HLA-B27 of human splenocytes and blood cells reveal a similar but partially different profile compared to in vitro grown cell lines
E Stodulkova, P Man, J Pohl, Nguyen D Van, S Vaingatova, E Ivaskova, M Pla, J Capkova, M Sedlackova, P Ivanyi, M Flieger
Language English Country Netherlands
Grant support
NI7327
MZ0
CEP Register
Digital library NLK
Full text - Část
Source
NLK
ScienceDirect (archiv)
from 1993-01-01 to 2009-12-31
- MeSH
- HLA-B27 Antigen chemistry immunology MeSH
- Cells, Cultured MeSH
- Humans MeSH
- Lymphocytes immunology MeSH
- Peptide Fragments chemistry immunology MeSH
- Spleen immunology MeSH
- Check Tag
- Humans MeSH
The sequences and profiles of peptides which bind to HLA-B*2705 splenocytes and peripheral blood cells were compared with those previously published from in vitro long-term cell cultures. B*2705 peptide profile analysed by solid-phase Edman degradation and 15 individual peptide sequences determined by LC-MS/MS were partially similar to those defined from in vitro long-term cell cultures. Arg at P2 was found in 11 of 15 sequenced peptides (73.3%). This value is lower in comparison with other published data. Two sequences were matching to unknown proteins, which displayed similarity with myosin. These are first data on peptide sequences isolated directly from HLA-B27 molecules without prior in vitro propagation of the cells.
Department of Rheumatology Thomayer Hospital Prague Czech Republic
Emory University School of Medicine Atlanta GA 30322 USA
Institute of Clinical and Experimental Medicine HLA Centre Prague Czech Republic
Institute of Microbiology Academy of Science of the Czech Republic
Institute of Molecular Genetics Academy of Science of the Czech Republic
Literatura
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- $a The sequences and profiles of peptides which bind to HLA-B*2705 splenocytes and peripheral blood cells were compared with those previously published from in vitro long-term cell cultures. B*2705 peptide profile analysed by solid-phase Edman degradation and 15 individual peptide sequences determined by LC-MS/MS were partially similar to those defined from in vitro long-term cell cultures. Arg at P2 was found in 11 of 15 sequenced peptides (73.3%). This value is lower in comparison with other published data. Two sequences were matching to unknown proteins, which displayed similarity with myosin. These are first data on peptide sequences isolated directly from HLA-B27 molecules without prior in vitro propagation of the cells.
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