Quantification of selenium-tagged proteins in human plasma using species-unspecific isotope dilution ICP-DRC-qMS coupled on-line with anion exchange chromatography

2008 ◽  
Vol 23 (11) ◽  
pp. 1545 ◽  
Author(s):  
Ming Xu ◽  
Limin Yang ◽  
Qiuquan Wang
Keyword(s):  
Human Plasma ◽  
Anion Exchange ◽  
Isotope Dilution ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
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Oligosaccharide analysis by capillary-scale high-pH anion-exchange chromatography with on-line ion-trap mass spectrometry

2005 ◽  
Vol 829 (1-2) ◽  
pp. 136-143 ◽  
Author(s):  
Cees Bruggink ◽  
Manfred Wuhrer ◽  
Carolien A.M. Koeleman ◽  
Victor Barreto ◽  
Yan Liu ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Anion Exchange ◽  
Ion Trap ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Ion Trap Mass Spectrometry ◽  
High Ph ◽  
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Abstract 411: An Anion-Exchange Chromatography Isolated Subfraction of Mouse Apolipoprotein A-I Is Unable to Activate Cellular Cholesterol Release from Mouse Peritoneal Macrophage Foam Cells

2012 ◽  
Vol 32 (suppl_1) ◽  
Author(s):  
Kuniko Okumura-Noji ◽  
Giorgio Cavigiolio ◽  
Rong Huang ◽  
W Sean Davidson ◽  
Nobukatsu Akita ◽  
...  
Keyword(s):  
Human Plasma ◽  
Anion Exchange ◽  
Cholesterol Efflux ◽  
Foam Cells ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Cellular Cholesterol ◽  
Mouse Plasma ◽  
Cellular Cholesterol Efflux ◽  
Human And Mouse

Aim: Human and mouse plasma apoA-I separate on anion exchange chromatography (6M urea) in distinct subfractions. To investigate the nature of this diversity, we analyzed the protein subfractions by IEF and Urea-PAGE, and compared their ability to generate HDL in vitro. Methods: Human and mouse plasma HDLs were delipidated then applied to an DE52 ion-exchange column and eluted by 30-60mM Tris-HCl, pH7.80 containing 6M urea. Mouse, human, and recombinant apoA-Is were analyzed by IEF (Ettan IPGphor3) followed by CBB protein staining. Urea-PAGE analysis was performed with 14% acrylamide gel in 6M urea buffer. ApoA-Is abilities to efflux cholesterol from mouse peritoneal foam cells and to shift the size of the ACAT-accessible cholesterol pool were determined. Results: Human plasma and recombinant human apoA-I showed two apoA-I subtypes by IEF and Urea-PAGE analysis; whereas HDL from C57BL/6 and 129SV mice contained three apoA-Is at pI=5.37, 5.31, 5.27 (mP3-1, mP2, mP3-3), and pI=5.44, 5.37, 5.32, respectively. Subfractions mP2 and mP3-3 were isolated on a DE52 column and, despite their difference in pI, were able to mediate cellular cholesterol efflux at levels similar to human plasma apoA-Is. Subfraction mP3-1, with the highest pI, eluted between mP2 and mP3-3 on DE-52 column. Interestingly, for both mouse strains, mP3-1 showed very poor cholesterol efflux and the incorporation of 14C-oleic acid to cellular CE was significantly higher when compared to mP2 and mP3-3. Conclusion: We found that differences in the pI of anion-exchange chromatography apoA-I subfractions did not directly affect HDL generation except for mouse subtype mP3-1. mP3-1 binds strongly to the anionic DE52 resin, probably by hydrophobic interaction, and is unable to mediate cellular cholesterol efflux. Further investigation of the nature of the differences in these apoA-I subtypes will provide insights on factors that may be implicated in the biogenesis of HDL in vivo.

Characterisation of two novel cyclodextrinases using on-line microdialysis sampling with high-performance anion exchange chromatography

2006 ◽  
Vol 385 (8) ◽  
pp. 1421-1429 ◽  
Author(s):  
Carina Nilsson ◽  
Frida Nilsson ◽  
Pernilla Turner ◽  
Martin Sixtensson ◽  
Eva Nordberg Karlsson ◽  
...  
Keyword(s):  
Anion Exchange ◽  
High Performance ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Microdialysis Sampling ◽  
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