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Enrichment of human brain proteins by heparin chromatography
Author(s) -
Karlsson Krister,
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(19991001)20:14<2970::aid-elps2970>3.0.co;2-p
Subject(s) - heparin , chemistry , matrix assisted laser desorption/ionization , proteomics , chromatography , biochemistry , gel electrophoresis , mass spectrometry , enzyme , adsorption , desorption , gene , organic chemistry
Detection of low‐abundance proteins is essential for the identification of novel drug targets by differential protein expression studies. We studied the enrichment of human fetal brain proteins by heparin chromatography. Total soluble brain proteins were fractionated on Heparin‐Actigel and the fractions collected were analyzed by two‐dimensional electrophoresis. The proteins were identified by matrix‐assisted laser desorption ionization mass spectrometry. Approximately 300 protein spots were analyzed, representing 70 different polypeptides, 50 of which were bound to the heparin matrix. Eighteen brain proteins were identified for the first time. The proteins enriched by heparin chromatography include both minor and major components of the brain protein extract. The enriched proteins belong to several classes, including proteasome components, dihydropirimidinase‐related proteins, T‐complex protein 1 components and enzymes with various catalytic activities. The results include a two‐dimensional map of the soluble brain proteins and a list of the proteins enriched by heparin chromatography. These may be useful in the design of protein purification protocols and in studies of neurological disorders.