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Matches in SemOpenAlex for { <https://semopenalex.org/work/W1999804530> ?p ?o ?g. }

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• W1999804530 abstract "We describe a microspot matrix-assisted laser desorption ionization (MALDI) mass spectrometric approach to analyze gel-separated phosphoproteins. This method involves in-gel digestion of phosphoproteins after gel separation, followed by open tubular capillary (OTC) immobilized metal-ion affinity chromatography (IMAC) to capture the phosphopeptides with markedly reduced interferences from nonphosphorylated peptides. Nanoliter-volume of ammonium phosphate is used to elute the phosphopeptides captured on the capillary tube. After mixing with a small volume of matrix solution in the capillary, the effluent is deposited in a microspot on a sample plate for MALDI−MS analysis. It is also shown that, with peptide esterification after in-gel digestion of a phosphoprotein, negative ion detection in MALDI gives a distinct advantage over the positive ion mode of operation for phosphopeptide analysis, even without IMAC enrichment. However, the OTC−IMAC technique is demonstrated to be superior to the approach of negative ion detection of esterified in-gel digests without IMAC. OTC−IMAC is found to be sufficiently selective to capture phosphopeptides from in-gel digest of a gel band containing predominately one protein and the combination of peptide esterification and IMAC enrichment does not provide any real advantage. Using a standard phosphoprotein α-casein as a model system, we demonstrate that this OTC−IMAC method can detect a number of phosphopeptides after in-gel digestion with mid-fmol protein sample loading. An example of real world applications of this method is illustrated in the characterization of a fusion protein, His182, expressed in E. coli. Keywords: phosphoprotein • open tubular column • IMAC • MALDI" @default.
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• W1999804530 date "2005-03-04" @default.
• W1999804530 modified "2023-09-23" @default.
• W1999804530 title "Nanoliter Sample Handling Combined with Microspot MALDI−MS for Detection of Gel-Separated Phosphoproteins" @default.
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• W1999804530 doi "https://doi.org/10.1021/pr049789t" @default.
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