Global mapping of rat plasma proteins with a native proteomic approach using nondenaturing micro 2DE and quantitative LC-MS/MS

2016 ◽  
Vol 37 (23-24) ◽  
pp. 3126-3136
Author(s):  
Shumin Chen ◽  
Meiling Wen ◽  
Shujie Bu ◽  
Ahui Wang ◽  
Ya Jin ◽  
...  
2007 ◽  
Vol 30 (12) ◽  
pp. 1979-1988 ◽  
Author(s):  
Md Imtaiyaz Hassan ◽  
Vijay Kumar ◽  
Tara Kashav ◽  
Neelima Alam ◽  
Tej P. Singh ◽  
...  

1971 ◽  
Vol 60 (11) ◽  
pp. 1642-1646 ◽  
Author(s):  
Gordon J. Conard ◽  
Coryce O. Haavik ◽  
Kenneth F. Finger

1962 ◽  
Vol 40 (2) ◽  
pp. 153-157 ◽  
Author(s):  
Anita Berecz ◽  
C. Godin

When 7-azatryptophan and 5-methyltryptophan are fed to protein-depleted rats, the animals lose weight more rapidly than control rats. Protein-depleted rats fed a diet containing tryptophan gain weight. 7-Azatryptophan is incorporated in vivo into rat plasma proteins, whereas 5-methyltryptophan is not incorporated.


PROTEOMICS ◽  
2009 ◽  
Vol 9 (1) ◽  
pp. 148-158 ◽  
Author(s):  
Fabrice Bertile ◽  
Christine Schaeffer ◽  
Yvon Le Maho ◽  
Thierry Raclot ◽  
Alain Van Dorsselaer

2009 ◽  
Vol 92 (6) ◽  
pp. 1652-1657 ◽  
Author(s):  
Susantha Mohottalage ◽  
Renaud Vincent ◽  
Prem Kumarathasan

Abstract Plasma is a complex matrix and has to be clarified or fractionated to obtain informative MS data. Although there are a number of prefractionation methods to clean up complex biological matrixes before proteomic analysis, these methods require large sample volumes and are costly and time-consuming. Alternatively, recently introduced magnetic beads (MB) appear to be attractive in overcoming these difficulties. Therefore, we were interested in investigating the applicability of MB in the clarification of rat plasma samples for proteome analyses. For this purpose, we used complementary supports, such as hydrophobic interaction chromatography-based MB (MB-C18) and weak cation-exchange chromatography-based MB (MB-WCX). MB-based fractionated samples were either spotted directly or underwent tryptic digestion before matrix-assisted laser desorption ionization (MALDI) spotting. Samples from both MB separation techniques gave clean and well-resolved MALDI-time-of-flight MS spectra in the low molecular mass range of 110 kDa with -cyano-4-hydroxycinnamic acid as the matrix. Both techniques gave approximately 300 analyte peaks in this mass range. Our results showed that both MB-based separation procedures gave complementary mass spectral information. This approach provided information on the identity of a number of less-abundant and more-abundant proteins in plasma. Our findings suggest that this MB-based proteomic approach can be valuable in conducting faster screening of plasma samples for protein profiling.


2012 ◽  
Vol 75 (4) ◽  
pp. 1386-1400 ◽  
Author(s):  
Jung-Won Choi ◽  
Hao Liu ◽  
Duk Kwon Choi ◽  
Tae Seok Oh ◽  
Rajib Mukherjee ◽  
...  

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