Digestion of Insoluble Protein Fractions for Multidimensional Protein Identification Technology (MuDPIT) Analysis

2006 ◽  
Vol 2006 (28) ◽  
pp. pdb.prot4556-pdb.prot4556
Author(s):  
D. M. Schieltz ◽  
M. P. Washburn
2020 ◽  
Vol 31 (7) ◽  
pp. 1440-1447
Author(s):  
Nan Zhang ◽  
Xiaojing Liu ◽  
Shuaixin Gao ◽  
Catherine Chiulan Wong

PROTEOMICS ◽  
2006 ◽  
Vol 6 (1) ◽  
pp. 301-311 ◽  
Author(s):  
Emmanuelle M. Bayer ◽  
Andrew R. Bottrill ◽  
John Walshaw ◽  
Marielle Vigouroux ◽  
Mike J. Naldrett ◽  
...  

2002 ◽  
Vol 74 (7) ◽  
pp. 1650-1657 ◽  
Author(s):  
Michael P. Washburn ◽  
Ryan Ulaszek ◽  
Cosmin Deciu ◽  
David M. Schieltz ◽  
John R. Yates

2008 ◽  
Vol 75 (2) ◽  
pp. 366-373 ◽  
Author(s):  
Janet R. Donaldson ◽  
Bindu Nanduri ◽  
Shane C. Burgess ◽  
Mark L. Lawrence

ABSTRACT Listeria monocytogenes is a gram-positive, food-borne pathogen that causes disease in both humans and animals. There are three major genetic lineages of L. monocytogenes and 13 serovars. To further our understanding of the differences that exist between different genetic lineages/serovars of L. monocytogenes, we analyzed the global protein expression of the serotype 1/2a strain EGD and the serotype 4b strain F2365 during early-stationary-phase growth at 37°C. Using multidimensional protein identification technology with electrospray ionization tandem mass spectrometry, we identified 1,754 proteins from EGD and 1,427 proteins from F2365, of which 1,077 were common to both. Analysis of proteins that had significantly altered expression between strains revealed potential biological differences between these two L. monocytogenes strains. In particular, the strains differed in expression of proteins involved in cell wall physiology and flagellar biosynthesis, as well as DNA repair proteins and stress response proteins.


1967 ◽  
Vol 105 (2) ◽  
pp. 605-609 ◽  
Author(s):  
C B Taylor ◽  
E. Bailey ◽  
W Bartley

1. Male rats were injected intraperitoneally with l-[35S]methionine, [32P]-phosphate and [2−14C]acetate. The animals were killed at various times up to 72hr. after injection, and liver mitochondria were prepared and fractionated into soluble protein, insoluble protein and lipid for assay of the radioactivity of each fraction. 2. The maximal specific radioactivity of total mitochondrial phospholipid with respect to both 32P and 14C was attained after approx. 6hr. 3. 32P was incorporated most rapidly into phosphatidylethanolamine, maximal incorporation being attained after approx. 6hr.; maximal incorporation into lecithin occurred after 6–12hr. The specific radioactivity of cardiolipin was still slowly increasing at the end of the experiment (72hr.). 4. There were no major differences between the rates of incorporation of 14C into the lecithin, phosphatidylethanolamine and cardiolipin fractions of mitochondrial phospholipid, maximal incorporation in each case occurring after approx. 6hr. 5. Maximal incorporation of 35S into both soluble and insoluble protein fractions was attained less than 12hr. after injection, the maximal specific radioactivity of soluble protein being higher than that of insoluble protein.


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