Premium
Web‐based two‐dimensional database of Saccharomyces cerevisiae proteins using immobilized pH gradients from pH 6 to pH 12 and matrix‐assisted laser desorption/ionization‐time of flight mass spectrometry
Author(s) -
Wildgruber Robert,
Reil Gerold,
Drews Oliver,
Parlar Harun,
Görg Angelika
Publication year - 2002
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/1615-9861(200206)2:6<727::aid-prot727>3.0.co;2-2
Subject(s) - mass spectrometry , immobilized ph gradient , isoelectric focusing , chromatography , isoelectric point , chemistry , time of flight mass spectrometry , desorption , matrix assisted laser desorption/ionization , protein mass spectrometry , matrix (chemical analysis) , analytical chemistry (journal) , ionization , biochemistry , electrospray ionization , ion , organic chemistry , adsorption , enzyme
An image based two‐dimensional (2‐D) reference map of very alkaline yeast cell proteins was established by using immobilized pH gradients (IPG) up to pH 12 (IPG 6–12, IPG 9–12 and IPG 10–12) for 2‐D electrophoresis and by using matrix‐assisted laser desorption/ionization‐time of flight mass spectrometry peptide mass fingerprinting for spot identification. Up to now 106 proteins with theoretical isoelectric points up to pH 11.15 and molecular mass between 7.5 and 115 kDa were localized and identified. Additionally, due to the improved resolution of steady‐state isoelectric focussing with IPGs, even low copy number proteins with codon bias below 0.02 were detected and identified.