Interlaboratory comparative study of the numerical analysis of one-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoretic protein patterns of Campylobacter strains
โ Scribed by Dr. Menelaos Costas; Bruno Pot; Peter Vandamme; Karel Kersters; Robert J. Owen; Leslie R. Hill
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 952 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0173-0835
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โฆ Synopsis
Interlaboratory comparative study of the numerical analysis of one-dimensional sodium dodecyl sulphatepolyacrylamide gel electrophoretic protein patterns of Campylobacter strains
Twenty-nine bacterial strains of the genus Campylobacter were examined independently at two collaborating institutes, the National Collection of Type Cultures, London and the Laboratorium voor Microbiologie, Rijksuniversiteit Gent. The onedimensional polyacrylamide gel electrophoretic protein patterns of the strains were analysed using computerised numerical methods which employed a correlation coefficient and a clustering algorithm. The electrophoretic methods used at the two institutes included both major differences such as gel composition and running conditions and minor differences in buffer composition. Although the algorithm on which similarity and clustering were computed were the same, the detailed treatment of scan patterns differed. The resulting protein patterns in the gels differed markedly in appearance but after numerical analysis the t y o systems were equally effective in their ability to speciate the strains. There were, however, differences in the relationships between the species defined at the two institutes and these were at least partly due t o the different background subtraction methods employed. In conclusion, th.e portability and reproducibility ofthe two systems for identification was demonstrated but for definitive classification further standardization may be required.
๐ SIMILAR VOLUMES
Two mixtures of proteins having molecular weights in the range $8-97 kDa were separated by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and examined by delayed extraction matrix-assisted laser desorption/ionisation mass spectrometry (MALDI-MS). Part of our aim in this study