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On-line immobilized metal affinity chromatography/capillary electrophoresis/electrospray ionization-mass spectrometry (IMAC/CE/ESI-MS) offers selective preconcentration of phosphorylated peptides with identification of the phosphorylated amino acid(s). The preconcentration provides low concentration limits of detection and capillary electrophoresis separates the peptides. Recently, we reported a fast, simple, and sensitive on-line IMAC/CE/ESI-MS/MS method for the determination of phosphopeptides at low-pmole levels. That work is expanded here by use of multiple stage tandem mass spectrometry (MS(n), n = 2,3) to isolate and fragment target ions to provide more reliable assignments of phosphorylated residues. The application of IMAC/CE/ESI-MS(n) is demonstrated by the analysis of tryptic digests of alpha- and beta-casein and in-gel tryptic digests of beta-casein. 相似文献
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The analysis of large phosphoproteins by mass spectrometry is a particular challenge, in many cases, because of the small proportion of phosphopeptides in the presence of a large number of non-phosphorylated peptides. In addition, phosphopeptides are generally available in dilute solutions. Thus, methods to specifically identify phosphopeptides at low concentrations are important. In this work, on-line Fe(III) immobilized metal-ion affinity chromatography (IMAC)-CE-electrospray ionization MS was developed and applied to sub-pmol analysis of phosphopeptides. Phosphopeptides bind Fe(III) with high selectivity. The IMAC resin is packed directly at the head of the CE column. After the phosphopeptides are bonded to the resin and washed, they are eluted at high pH and separated by CE. This method has several advantages: (1) selective retention and pre-concentration of phosphopeptides on an Fe(III)-IMAC resin; (2) a pre-wash of the sample to remove salts and buffers that are not suited for CE separation or ESI operation; (3) facile fabrication with common tools and chemicals (less than 10 min); (4) adaptation to commercial CE instruments without any modifications. The applications of IMAC-CE-MS are demonstrated by the analysis of phosphopeptide mixtures and a phosphoprotein digest. 相似文献
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Computer simulations based on Discrete Element Method have been performed in order to investigate the influence of interparticle interactions on the kinetics of self-assembly and the mechanical strength of nanoparticle aggregates.Three different systems have been considered.In the first system the interaction between particles has been simulated using the JKR (Johnson,Kendall and Roberts) contact theory,while in the second and third systems the interaction between particles has been simulated using van der Waals and electrostatic forces respectively.In order to compare the mechanical behaviour of the three systems,the magnitude of the maximum attractive force between particles has been kept the same in all cases.However,the relationship between force and separation distance differs from case to case and thus,the range of the interparticle force.The results clearly indicate that as the range of the interparticle force increases,the self-assembly process is faster and the work required to produce the mechanical failure of the assemblies increases by more than one order of magnitude. 相似文献
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An automated, sheathless capillary electrophoresis-mass spectrometry platform for discovery of biomarkers in human serum 总被引:1,自引:0,他引:1
Sassi AP Andel F Bitter HM Brown MP Chapman RG Espiritu J Greenquist AC Guyon I Horchi-Alegre M Stults KL Wainright A Heller JC Stults JT 《Electrophoresis》2005,26(7-8):1500-1512
A capillary electrophoresis-mass spectrometry (CE-MS) method has been developed to perform routine, automated analysis of low-molecular-weight peptides in human serum. The method incorporates transient isotachophoresis for in-line preconcentration and a sheathless electrospray interface. To evaluate the performance of the method and demonstrate the utility of the approach, an experiment was designed in which peptides were added to sera from individuals at each of two different concentrations, artificially creating two groups of samples. The CE-MS data from the serum samples were divided into separate training and test sets. A pattern-recognition/feature-selection algorithm based on support vector machines was used to select the mass-to-charge (m/z) values from the training set data that distinguished the two groups of samples from each other. The added peptides were identified correctly as the distinguishing features, and pattern recognition based on these peptides was used to assign each sample in the independent test set to its respective group. A twofold difference in peptide concentration could be detected with statistical significance (p-value < 0.0001). The accuracy of the assignment was 95%, demonstrating the utility of this technique for the discovery of patterns of biomarkers in serum. 相似文献
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在一系列H模放电条件下,建立了一个旨在研究等离子体温度分布剖面不变性的数据库。介绍了数据库建立过程中要解决的关键问题和所用软件,对等离子体温度分布剖面不变性及芯部约束与边缘参数的关系进行了研究。 相似文献
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John J. D'Amico B. Ray Stults Peter G. Ruminski Karl V. Wood 《Journal of heterocyclic chemistry》1983,20(5):1283-1286
The reaction of o-phthaldehyde with potassium cyanide and methylamine hydrochloride afforded 1-cyano-2-methylisoindole ( 1 ) in 92% yield. Possible mechanism and supporting nmr, ir, mass spectrum and single X-ray structure analysis for 1 are discussed. The X-ray study revealed that the true structure of 1 can best be represented as a resonance hybrid of the canonical forms a, b, c and d . 相似文献