Volumetric Mass Spectrometry Protein Arrays

2007 ◽  
pp. 333-343 ◽  
Author(s):  
Dobrin Nedelkov ◽  
Urban A. Kiernan ◽  
Eric E. Niederkofler ◽  
Kemmons A. Tubbs ◽  
Randall W. Nelson
Keyword(s):  
Mass Spectrometry ◽  
Protein Arrays

scholarly journals Protein Arrays as Tools for Detection of Protein-Protein Interactions by Mass Spectrometry

2010 ◽  
pp. 725-727
Author(s):  
Christian F. W. Becker ◽  
Ron Wacker ◽  
Werner Bouschen ◽  
Ralf P. Seidel ◽  
Branko Kolaric ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Protein Arrays

scholarly journals Reconstructed protein arrays from 3D HPLC/tandem mass spectrometry and 2D gels: complementary approaches to Porphyromonas gingivalis protein expression

The Analyst ◽  
2002 ◽  
Vol 127 (11) ◽  
pp. 1450-1456 ◽  
Author(s):  
Tiansong Wang ◽  
Yi Zhang ◽  
Weibin Chen ◽  
Yoonsuk Park ◽  
Richard J. Lamont ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Protein Expression ◽  
Porphyromonas Gingivalis ◽  
Tandem Mass ◽  
Protein Arrays

Protein Arrays on Patterned Porous Gold Substrates Interrogated with Mass Spectrometry:  Detection of Peptides in Plasma

2008 ◽  
Vol 80 (5) ◽  
pp. 1448-1458 ◽  
Author(s):  
Kenyon M. Evans-Nguyen ◽  
Sheng-Ce Tao ◽  
Heng Zhu ◽  
Robert J. Cotter
Keyword(s):  
Mass Spectrometry ◽  
Mass Spectrometry Detection ◽  
Protein Arrays ◽  
Porous Gold ◽  
Gold Substrates

Optimization and evaluation of surface-enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF MS) with reversed-phase protein arrays for protein profiling

2005 ◽  
Vol 43 (2) ◽  
Author(s):  
Manuel Aivado ◽  
Dimitrios Spentzos ◽  
Gil Alterovitz ◽  
Hasan H. Otu ◽  
Franck Grall ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Time Of Flight ◽  
Laser Desorption ◽  
Laser Desorption Ionization ◽  
Protein Profiles ◽  
Protein Arrays ◽  
Desorption Ionization ◽  
Flight Mass Spectrometry ◽  
Surface Enhanced

AbstractSurface-enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry with protein arrays has facilitated the discovery of disease-specific protein profiles in serum. Such results raise hopes that protein profiles may become a powerful diagnostic tool. To this end, reliable and reproducible protein profiles need to be generated from many samples, accurate mass peak heights are necessary, and the experimental variation of the profiles must be known. We adapted the entire processing of protein arrays to a robotics system, thus improving the intra-assay coefficients of variation (CVs) from 45.1% to 27.8% (p<0.001). In addition, we assessed up to 16 technical replicates, and demonstrated that analysis of 2–4 replicates significantly increases the reliability of the protein profiles. A recent report on limited long-term reproducibility seemed to concord with our initial inter-assay CVs, which varied widely and reached up to 56.7%. However, we discovered that the inter-assay CV is strongly dependent on the drying time before application of the matrix molecule. Therefore, we devised a standardized drying process and demonstrated that our optimized SELDI procedure generates reliable and long-term reproducible protein profiles with CVs ranging from 25.7% to 32.6%, depending on the signal-to-noise ratio threshold used.

Comparison of Conventional and Electron Spectroscopic Imaging in the Fixed Beam Electron Microscope of Ordered Protein Arrays

1985 ◽  
Vol 43 ◽  
pp. 74-75
Author(s):  
E. L. Buhle ◽  
U. Aebi
Keyword(s):  
Image Processing ◽  
Electron Microscope ◽  
High Resolution ◽  
Image Plane ◽  
Electron Spectroscopic Imaging ◽  
Protein Arrays ◽  
Beam Electron ◽  
Average Unit ◽  
Fixed Beam ◽  
Energy Components

CTEM brightfield images are formed by a combination of relatively high resolution elastically scattered electrons and unscattered and inelastically scattered electrons. In the case of electron spectroscopic images (ESI), the inelastically scattered electrons cause a loss of both contrast and spatial resolution in the image. In the case of ESI imaging on the Zeiss EM902, the transmited electrons are dispersed into their various energy components by passing them through a magnetic prism spectrometer; a slit is then placed in the image plane of the prism to select the electrons of a given energy loss for image formation. The purpose of this study was to compare CTEM with ESI images recorded on a Zeiss EM902 of ordered protein arrays. Digital image processing was employed to analyze the average unit cell morphologies of the two types of images.

How SIMS microscopy can be used in medicine

1992 ◽  
Vol 50 (2) ◽  
pp. 1602-1603
Author(s):  
Philippe Fragu
Keyword(s):  
Mass Spectrometry ◽  
Biomedical Applications ◽  
Secondary Ion Mass Spectrometry ◽  
Chemical Elements ◽  
Biological Applications ◽  
The Past ◽  
Potential Source ◽  
Secondary Ion ◽  
Chemical Integrity ◽  
Scientific Endeavour

The identification, localization and quantification of intracellular chemical elements is an area of scientific endeavour which has not ceased to develop over the past 30 years. Secondary Ion Mass Spectrometry (SIMS) microscopy is widely used for elemental localization problems in geochemistry, metallurgy and electronics. Although the first commercial instruments were available in 1968, biological applications have been gradual as investigators have systematically examined the potential source of artefacts inherent in the method and sought to develop strategies for the analysis of soft biological material with a lateral resolution equivalent to that of the light microscope. In 1992, the prospects offered by this technique are even more encouraging as prototypes of new ion probes appear capable of achieving the ultimate goal, namely the quantitative analysis of micron and submicron regions. The purpose of this review is to underline the requirements for biomedical applications of SIMS microscopy.Sample preparation methodology should preserve both the structural and the chemical integrity of the tissue.

Imaging of Al-Li-Cu alloys with a Scanning Ion Microprobe

1990 ◽  
Vol 48 (2) ◽  
pp. 314-315
Author(s):  
K.K. Soni ◽  
D.B. Williams ◽  
J.M. Chabala ◽  
R. Levi-Setti ◽  
D.E. Newbury
Keyword(s):  
Mass Spectrometry ◽  
Secondary Ion Mass Spectrometry ◽  
Equilibrium Phase ◽  
Icosahedral Symmetry ◽  
Ion Microprobe ◽  
X Ray ◽  
Cu Alloys ◽  
Two Phases ◽  
The University ◽  
Secondary Ion

In contrast to the inability of x-ray microanalysis to detect Li, secondary ion mass spectrometry (SIMS) generates a very strong Li+ signal. The latter’s potential was recently exploited by Williams et al. in the study of binary Al-Li alloys. The present study of Al-Li-Cu was done using the high resolution scanning ion microprobe (SIM) at the University of Chicago (UC). The UC SIM employs a 40 keV, ∼70 nm diameter Ga+ probe extracted from a liquid Ga source, which is scanned over areas smaller than 160×160 μm2 using a 512×512 raster. During this experiment, the sample was held at 2 × 10-8 torr.In the Al-Li-Cu system, two phases of major importance are T1 and T2, with nominal compositions of Al2LiCu and Al6Li3Cu respectively. In commercial alloys, T1 develops a plate-like structure with a thickness <∼2 nm and is therefore inaccessible to conventional microanalytical techniques. T2 is the equilibrium phase with apparent icosahedral symmetry and its presence is undesirable in industrial alloys.

Applications of Time-OF-Flight Secondary Ion Mass Spectrometry (TOF-SIMS)

1990 ◽  
Vol 48 (2) ◽  
pp. 308-309
Author(s):  
Bruno Schueler ◽  
Robert W. Odom
Keyword(s):  
Mass Spectrometry ◽  
Secondary Ion Mass Spectrometry ◽  
Structural Information ◽  
Time Of Flight ◽  
Biological Tissues ◽  
Polymer Surfaces ◽  
Tof Sims ◽  
Secondary Ions ◽  
Ion Mass Spectrometry ◽  
Secondary Ion

Time-of-flight secondary ion mass spectrometry (TOF-SIMS) provides unique capabilities for elemental and molecular compositional analysis of a wide variety of surfaces. This relatively new technique is finding increasing applications in analyses concerned with determining the chemical composition of various polymer surfaces, identifying the composition of organic and inorganic residues on surfaces and the localization of molecular or structurally significant secondary ions signals from biological tissues. TOF-SIMS analyses are typically performed under low primary ion dose (static SIMS) conditions and hence the secondary ions formed often contain significant structural information.This paper will present an overview of current TOF-SIMS instrumentation with particular emphasis on the stigmatic imaging ion microscope developed in the authors’ laboratory. This discussion will be followed by a presentation of several useful applications of the technique for the characterization of polymer surfaces and biological tissues specimens. Particular attention in these applications will focus on how the analytical problem impacts the performance requirements of the mass spectrometer and vice-versa.

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