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PeptideAtlas provides a multi-organism, publicly accessible compendium of peptides identified in a large set of tandem mass spectrometry proteomics experiments collected for human, mouse, yeast, and several other organisms.
(last updated: Nov 28, 2017)
Data or Model Molecule| Accession | Sample Title | Summary | Organism | Characteristics | Instrument | Treatment | |||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| PAe000151 | gricat | gricat Galactose vs. raffinose ICAT experiment Published in Trey's thesis | Yeast | BY4741 and nine mutants: gal1∆, gal2∆, gal3∆, gal4∆, gal5∆, gal6∆, gal7∆, gal10∆, gal80∆, Wild-type (wt) and nine genetically altered yeast strains were examined, each with a complete deletion of one of the nine GAL genes: transport (gal2∆), enzymatic (gal1∆, gal5∆, gal7∆, or gal10∆), or regulatory (gal3∆, gal4∆, gal6∆, or gal80∆).These strains were perturbed environmentally by growth in the presence (+gal) or absence(-gal) of 2% galactose, with 2% raffinose provided in both media. Strains were derived from the wild-type haploid MATa strain BY4741 (ATCC #201388, MATa his3∆1 leu2∆0 met15∆0 ura3∆0). The mutants gal1∆, gal3∆, gal5∆, gal7∆, and gal10∆ were constructed by complete replacement of the corresponding genes with kanR using the loxP-kanR-loxP cassette, while gal2∆, gal4∆, gal6∆, and gal80∆ were obtained from the Saccharomyces Genome Deletion Project and were constructed analogously. Strains gal2∆gal80∆ and gal4∆gal80∆ were obtained by mating and sporulation of the single-deletion mutants; gal1∆gal10∆ (#R4146) was a generous gift from C. Roberts of Rosetta Inpharmatics. | LTQ | Yeast were inoculated in 100 ml of either GAL inducing "+gal" media (1% yeast extract, 2% peptone,2% rafÞnose, 2% galactose) or noninducing "-gal" media (1% yeast extract, 2% peptone, 2% rafÞnose). Cultures were grown overnight at 30°C to a density of 1 to 2 OD₆₀₀, washed in 5 ml H₂O, and snap-frozen. | Equal amounts of protein extracts from wt+gal (galactose utilization) and wt–gal cultures were labeled with isotopically heavy and normal ICAT reagents, respectively, then combined and digested with trypsin. | Protein extracts were desalted (Biorad 10DG columns) in 50 mM tris 8.3, 1 mM EDTA, and 0.05% SDS. The ICAT method was applied to 300 µg of protein from each extract, with the following modification. After trypsin digestion, peptides were fractionated on a 2.1 mm by 200 mm polySULFOETHYL A column (PolyLC) by running a salt gradient from 0 to 25% Buffer B (5 mM KH₃PO₄, pH 3.0, 350 mM KCl, 25% CH₃CN) over 30 min, followed by 25 to 100% Buffer B over 20 min at 0.2 ml/min. | Labeled peptides were isolated from each cation-exchange-chromatography, fraction by monomeric avidin (Pierce) affnity chromatography. | PMID:11340206 |
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