scholarly journals Optimization of MALDI-TOF MS Detection for Enhanced Sensitivity of Affinity-Captured Proteins Spanning a 100 kDa Mass Range

2007 ◽  
Vol 6 (11) ◽  
pp. 4517-4524 ◽  
Author(s):  
Christine L. Gatlin-Bunai ◽  
Lisa H. Cazares ◽  
William E. Cooke ◽  
Oliver J. Semmes ◽  
Dariya I. Malyarenko
Talanta ◽  
2019 ◽  
Vol 200 ◽  
pp. 288-292 ◽  
Author(s):  
Shuping Long ◽  
Qin Qin ◽  
Yuning Wang ◽  
Yi Yang ◽  
Yan Wang ◽  
...  

2008 ◽  
Vol 6 (4) ◽  
pp. 654-661 ◽  
Author(s):  
N. Cioffi ◽  
F. De Palo ◽  
C. D. Calvano ◽  
I. D. van der Werf ◽  
F. Palmisano ◽  
...  

2005 ◽  
Vol 4 (5) ◽  
pp. 1863-1866 ◽  
Author(s):  
Laurie L. Parker ◽  
Alexander B. Schilling ◽  
Stephen J. Kron ◽  
Stephen B. H. Kent
Keyword(s):  

2017 ◽  
Vol 137 ◽  
pp. 30-33 ◽  
Author(s):  
Veronika Rotova ◽  
Costas C. Papagiannitsis ◽  
Anna Skalova ◽  
Katerina Chudejova ◽  
Jaroslav Hrabak
Keyword(s):  

The Analyst ◽  
2004 ◽  
Vol 129 (9) ◽  
pp. 817 ◽  
Author(s):  
Xiaoyan Zhao ◽  
Jennifer Barber-Singh ◽  
Scott A. Shippy
Keyword(s):  

2010 ◽  
Vol 4 (1) ◽  
pp. 108-115 ◽  
Author(s):  
Violeta Ivanova ◽  
Ágnes Dörnyei ◽  
Marina Stefova ◽  
Trajće Stafilov ◽  
Borimir Vojnoski ◽  
...  
Keyword(s):  

2005 ◽  
Vol 51 (6) ◽  
pp. 973-980 ◽  
Author(s):  
Sven Baumann ◽  
Uta Ceglarek ◽  
Georg Martin Fiedler ◽  
Jan Lembcke ◽  
Alexander Leichtle ◽  
...  

Abstract Background: Magnetic bead purification for the analysis of low-abundance proteins in body fluids facilitates the identification of potential new biomarkers by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). The aims of our study were to establish a proteome fractionation technique and to validate a standardized blood sampling, processing, and storage procedure for proteomic pattern analysis. Methods: We used magnetic bead separation for proteome profiling of human blood by MALDI-TOF MS (mass range, 1000–10 000 Da) and studied the effects on the quality and reproducibility of the proteome analysis of anticoagulants, blood clotting, time and temperature of sample storage, and the number of freeze–thaw cycles of samples. Results: The proteome pattern of human serum was characterized by ∼350 signals in the mass range of 1000–10 000 Da. The proteome profile showed time-dependent dynamic changes before and after centrifugation of the blood samples. Serum mass patterns differed between native samples and samples frozen once. The best reproducibility of proteomic patterns was with a single thawing of frozen serum samples. Conclusion: Application of the standardized preanalytical blood sampling and storage procedure in combination with magnetic bead-based fractionation decreases variability of proteome patterns in human serum assessed by MALDI-TOF MS.


2020 ◽  
Vol 8 (1) ◽  
pp. 38-44 ◽  
Author(s):  
Sivakumar Palanisamy ◽  
Shuai Huang ◽  
Huiyuan Zhao ◽  
Di Zhu ◽  
Xiaozhe Zhang

Rapid MALDI-TOF-MS detection of neurotransmitters in mice brain tissue extracts using triphenylphosphine gold(i) salt as an efficient matrix.


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