NDLI: 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.

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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.

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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.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Emory, Joshua F. Walworth, Matthew J. Van Berkel, Gary J. Schulz, Michael Minarik, Susanne
Description	Country affiliation: United States Author Affiliation: Emory JF ( Organic and Biological Mass Spectrometry Group, Chemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831-6131, USA.)
Abstract	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 0.1M 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.
File Format	HTM / HTML
ISSN	14690667
Issue Number	1
Volume Number	16
e-ISSN	17516838
Journal	European Journal of Mass Spectrometry
Language	English
Publisher	Sage Publications
Publisher Date	2010-01-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Analytical Discipline Chemistry Techniques Chromatography, High Pressure Liquid Methods Chromatography, Reverse-phase Chromatography, Thin Layer Proteins Analysis Spectrometry, Mass, Electrospray Ionization Amino Acid Sequence Animals Caseins Isolation & Purification Cattle Chickens Instrumentation Cytochromes c Equipment Design Horses Molecular Sequence Data Muramidase Myoglobin Serum Albumin, Bovine Evaluation Studies Journal Article Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Medicine Atomic and Molecular Physics, and Optics

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