@article{Bai2007alveo-9942,
  year={2007},
  title={Lung alveolar proteomics of bronchoalveolar lavage from a pulmonary alveolar proteinosis patient using high-resolution FTICR mass spectrometry},
  number={4},
  volume={389},
  issn={1618-2642},
  journal={Analytical and bioanalytical chemistry},
  pages={1075--1085},
  author={Bai, Yu and Galetskiy, Dmitry and Damoc, Eugen and Ripper, Jan and Woischnik, Markus and Griese, Matthias and Liu, Zhiqiang and Liu, Shuying and Przybylski, Michael}
}

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    <dc:contributor>Griese, Matthias</dc:contributor>
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    <dc:contributor>Damoc, Eugen</dc:contributor>
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    <dc:contributor>Ripper, Jan</dc:contributor>
    <dcterms:bibliographicCitation>First publ. in: Analytical and bioanalytical chemistry 389 (2007), 4, pp. 1075-1085</dcterms:bibliographicCitation>
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    <dcterms:title>Lung alveolar proteomics of bronchoalveolar lavage from a pulmonary alveolar proteinosis patient using high-resolution FTICR mass spectrometry</dcterms:title>
    <dc:creator>Griese, Matthias</dc:creator>
    <dcterms:abstract xml:lang="eng">High-resolution Fourier transform ion cyclotron resonance (FTICR) mass spectrometry was developed and applied to the proteome analysis of bronchoalveolar lavage fluid (BALF) from a patient with pulmonary alveolar proteinosis. With use of 1-D and 2-D gel electrophoresis, surfactant protein A (SP-A) and other surfactant-related lung alveolar proteins were efficiently separated and identified by matrix-assisted laser desorption/ionization FTICR mass spectrometry . Low molecular mass BALF proteins were separated using a gradient 2-D gel. An efficient extraction/precipitation system was developed and used for the enrichment of surfactant proteins. The result of the BALF proteome analysis show the presence of several isoforms of SP-A, in which an N-non-glycosylierte form and several proline hydroxylations were identified. Furthermore, a number of protein spots were found to contain a mixture of proteins unresolved by 2-D gel electrophoresis, illustrating the feasibility of high-resolution mass spectrometry to provide identifications of proteins that remain unseparated in 2-D gels even upon extended pH gradients.</dcterms:abstract>
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    <dc:creator>Damoc, Eugen</dc:creator>
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