Dataset Information

Human Plasma Gel Filtration Fractions MS Data

ABSTRACT: Mapping Atheroprotective Functions and Related Proteins/Lipoproteins in Size Fractionated Human Plasma

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

SUBMITTER: Debi Swertfeger

LAB HEAD: L. Jason Lu

PROVIDER: PXD005520 | Pride | 2017-02-23

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Data020314_01 (F019537).mzid_Data020314_01_(F019537).pride.mgf.gz	Mzid
	Data020314_01 (F019537).pride.mztab.gz	Mztab
	Data020314_01.wiff	Wiff
	Data020314_01.wiff.scan	Wiff
	Data020314_01F019537.mzid.gz	Mzid

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Publications

Mapping Atheroprotective Functions and Related Proteins/Lipoproteins in Size Fractionated Human Plasma.

Swertfeger Debi K DK Li Hailong H Rebholz Sandra S Zhu Xiaoting X Shah Amy S AS Davidson W Sean WS Lu Long J LJ

Molecular & cellular proteomics : MCP 20170221 4

HDL has been shown to possess a variety of cardio-protective functions, including removal of excess cholesterol from the periphery, and inhibition of lipoprotein oxidation. It has been proposed that various HDL subparticles exist, each with distinct protein and lipid compositions, which may be responsible for HDL's many functions. We hypothesized that HDL functions will co-migrate with the operational lipoprotein subspecies when separated by gel filtration chromatography. Plasma from 10 healthy ...[more]

PMID: 28223350

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Project description:BackgroundCertain wheat gluten proteins form large protein polymers that are extractable in 0.5% SDS only after sonication. Although there is a strong relationship between the amounts of these polymers in the flour and bread-making quality, the protein components of these polymers have not been thoroughly investigated.ResultsFlour proteins from the US bread wheat Butte 86 were extracted in 0.5% SDS using a two-step procedure with and without sonication. Proteins were further separated by size exclusion chromatography (SEC) into monomeric and polymeric fractions and analyzed by quantitative two-dimensional gel electrophoresis (2-DE). When proteins in select 2-DE spots were identified by tandem mass spectrometry (MS/MS), overlapping spots from the different protein fractions often yielded different identifications. Most high-molecular-weight glutenin subunits (HMW-GS) and low-molecular-weight glutenin subunits (LMW-GS) partitioned into the polymer fractions, while most gliadins were found in the monomer fractions. The exceptions were alpha, gamma and omega gliadins containing odd numbers of cysteine residues. These proteins were detected in all fractions, but comprised the largest proportion of the SDS-extractable polymer fraction. Several types of non-gluten proteins also were found in the polymer fractions, including serpins, triticins and globulins. All three types were found in the largest proportions in the SDS-extractable polymer fraction.ConclusionsThis is the first study to report the accumulation of gliadins containing odd numbers of cysteine residues in the SDS-extractable glutenin polymer fraction, supporting the hypothesis that these gliadins serve as chain terminators of the polymer chains. These data make it possible to formulate hypotheses about how protein composition influences polymer size and structure and provide a foundation for future experiments aimed at determining how environment affects glutenin polymer distribution. In addition, the analysis revealed additional layers of complexity to the wheat flour proteome that should be considered when evaluating quantitative 2-DE data.