557064-50-3Relevant articles and documents
Efficient tryptic proteolysis accelerated by laser radiation for peptide mapping in proteome analysis
Yao, Guoping,Deng, Chunhui,Zhang, Xiangmin,Yang, Pengyuan
supporting information; experimental part, p. 8185 - 8189 (2011/02/22)
Back to basics: Coupled with MALDI-TOF MS, laser-assisted proteolysis (see schematic illustration) enabled rapid protein digestion and peptide mapping without the need for enzyme immobilization to increase the efficiency of tryptic digestion. Protein solutions containing trypsin were digested in less than a minute upon irradiation at 808 nm with a laser.
Direct analysis of reversed-phase high-performance thin layer chromatography separated tryptic protein digests using a liquid microjunction surface sampling probe/electrospray ionization mass spectrometry system
Emory, Joshua F.,Walworth, Matthew J.,Van Berkel, Gary J.,Schulz, Michael,Minarik, Susanne
experimental part, p. 21 - 33 (2010/10/21)
The sampling, ionization and detection of tryptic peptides separated in one-dimension on reversed-phase high-performance thin layer chromatography (HPTLC) plates was performed using liquid microjunction surface sampling probe electrospray ionization mass spectrometry. Tryptic digests of five proteins [cytochrome c, myoglobin, beta-casein, lysozyme and bovine serum albumin (BSA)] were spotted on reversed phase HPTLC RP-8 F254s and HPTLC RP-18 F254s plates. The plates were then developed using 70/30 methanol/water with 0.1 M ammonium acetate. A dual purpose extraction/electrospray solution containing 70/30/0.1 water/methanol/formic acid was infused through the sampling probe during analysis of the developed lanes. Both full scan mass spectra and data dependent tandem mass spectra were acquired for each development lane to detect and verify the peptide distributions. Data dependent tandem mass spectra provided both protein identification and sequence coverage information. Highest sequence coverages were achieved for cytochrome c and myoglobin (62.5% and 58.3%, respectively) on reversed phase RP-8 plates. While the tryptic peptides were separated enough for identification, the peptide bands did show some overlap with most peptides located in the lower half of the development lane. Proteins whose peptides were more separated gave higher sequence coverage. Larger proteins such as beta-casein and BSA which were spotted in lower relative amounts gave much lower sequence coverage than the smaller proteins. US Government 2009 All rights reserved.
COMPOUND FOR DERIVATIZING POLYPEPTIDES AND METHOD FOR SEQUENCING AND QUANTIFIFYING AMINO ACIDS IN POLYPEPTIDES USING THE SAME
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Page/Page column 25-26, (2008/06/13)
The present invention relates to a compound for N-terminal substitution of polypeptides which is used in sequencing and quantifying amino acids and a method for sequencing and quantifying an amino acid sequence using the same. The method for sequencing an
