The characterization of micro-organisms by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

. Their advice and encouragement have been greatly appreciated. I would like to thank Dr. Cameron M. Sullards and David Bostwick for their valuable support and insightful comments in the field of mass spectrometry. My special

A brief history of the development of electrospray ionization mass spectrometry in the author’s laboratory at Yale Uni-versity with reference to its roots in the work of Rayleigh,

extracellular polysaccharides, EPS, isolated from Butyrivibrio fibrisolvens strains I1 and 12. The main methods used, alone or in combination, for solving the structures have been chemical degradation procedures, mass spectrometry (MS) and nuclear magnetic resonance (NMR) spectroscopy

whole-cell lysates for unprocessed proteins using surface-enhanced laser desorption ionization–time of flight mass spectrometry (MS). Eight proteins between 4 and 14 kDa were confirmed as being unprocessed and containing the initiator methionine by adding back purified MAP to the preparations prior

Electrospray ionization-multistage tandem mass spectrometry of complex multitin organometallic compounds

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ow nloaded from 2 Hydrophobic proteins such as integral membrane proteins are difficult to separate, and therefore to study, at a proteomics level. However, the Asn-linked carbohydrates (N-glycans) contained in membrane glycoproteins are important in differentiation, embryogenesis, inflammation, cancer and metastasis, and other vital cellular processes. Thus, the identification of these proteins and their sites of glycosylation in a well characterized model organism is the first step towards understanding the mechanisms by which N-glycans and their associated proteins function in vivo. In this report a proteomics method recently developed by our group was applied to C.elegans extracts to identify 117 hydrophobic N-glycosylated proteins by analysis of 195 glycopeptides containing 199 Asn-linked oligosaccharides. Most of the proteins identified are involved in cell adhesion, metabolism, or the transport of small molecules. In addition, there are 18 proteins for which no function is known or predictable by sequence

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