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Two‐dimensional map of human brain proteins
Author(s) -
Langen Hanno,
Berndt Peter,
Röder Daniel,
Cairns Nigel,
Lubec Gert,
Fountoulakis Michael
Publication year - 1999
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/(sici)1522-2683(19990101)20:4/5<907::aid-elps907>3.0.co;2-a
Subject(s) - mass spectrometry , chemistry , gel electrophoresis , coomassie brilliant blue , enzyme , proteomics , biochemistry , biology , chromatography , staining , genetics , gene
Samples of human brain from the parietal cortex lobe were analyzed by two‐dimensional gel electrophoresis, using immobilized pH gradient strips covering the various pH regions. The protein spots were visualized with colloidal Coomassie blue stain and identified by matrix‐assisted laser desorption/ionization mass spectrometry. Approximately 400 spots were identified, corresponding to 180 different brain proteins. The list of identified proteins includes a large number of structural proteins and of enzymes or enzyme subunits with various catalytic activities. The majority of proteins are localized in the cytoplasma and in mitochondria. The two‐dimensional map may be useful as a reference database to study changes in the protein level caused by various disorders, such as Alzheimer's disease, major depression and schizophrenia.