Top down proteomics of human membrane proteins from enriched mitochondrial fractions.

Top down proteomics of human membrane proteins from enriched mitochondrial fractions.
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DOI:
10.1021/ac3031527
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发表时间:
2013-02-05
影响因子:
7.4
通讯作者:
Kelleher, Neil L.
Kelleher, Neil L.
中科院分区:
化学1区
文献类型:
--
作者:
Catherman, Adam D.;Li, Mingxi;Tran, John C.;Durbin, Kenneth R.;Compton, Philip D.;Early, Bryan P.;Thomas, Paul M.;Kelleher, Neil L.

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The interrogation of intact integral membrane proteins has long been a challenge for biological mass spectrometry. Here, we demonstrate the application of Top Down mass spectrometry to whole membrane proteins below 60 kDa with up to 8 transmembrane helices. Analysis of enriched mitochondrial membrane preparations from human cells yielded identification of 83 integral membrane proteins, along with 163 membrane-associated or soluble proteins, with a median q value of 3 × 10−10. An analysis of matching fragment ions demonstrated that significantly more fragment ions were found within transmembrane domains than would be expected based upon the observed protein sequence. Forty-six proteins from the complexes of oxidative phosphorylation were identified which exemplifies the increasing ability of Top Down Proteomics to provide extensive coverage in a biological network.
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