High pH reversed-phase chromatography as a superior fractionation scheme compared to off-gel isoelectric focusing for complex proteome analysis

PROTEOMICS ◽  
2013 ◽  
Vol 13 (20) ◽  
pp. 2956-2966 ◽  
Author(s):  
Derek R. Stein ◽  
Xiaojie Hu ◽  
Stuart J. McCorrister ◽  
Garrett R. Westmacott ◽  
Francis A. Plummer ◽  
...  
2010 ◽  
Vol 1217 (21) ◽  
pp. 3531-3537 ◽  
Author(s):  
David Gétaz ◽  
Mumun Gencoglu ◽  
Nicola Forrer ◽  
Massimo Morbidelli

2012 ◽  
Vol 9 (2) ◽  
pp. 129-134 ◽  
Author(s):  
Feng Yang ◽  
Yufeng Shen ◽  
David G Camp ◽  
Richard D Smith

2005 ◽  
Vol 26 (6) ◽  
pp. 1174-1188 ◽  
Author(s):  
Manfred Heller ◽  
Philippe E. Michel ◽  
Patrick Morier ◽  
David Crettaz ◽  
Christian Wenz ◽  
...  

1995 ◽  
Vol 41 (4) ◽  
pp. 532-536 ◽  
Author(s):  
U Turpeinen ◽  
I Sipilä ◽  
P Anttila ◽  
U Karjalainen ◽  
B Kuronen ◽  
...  

Abstract We here report the characteristics of two rare alpha-chain hemoglobin (Hb) variants. The variants were found during quantification of HbA1c by cation-exchange HPLC with the Diamat glycohemoglobin analyzer. They were further characterized by isoelectric focusing and PolyCAT A cation-exchange chromatography. The structure of the abnormal Hbs was established by amino acid analysis after separation of the globin chains by reversed-phase chromatography, digestion with trypsin, separation of the peptides by reversed-phase chromatography, and amino acid sequencing. These studies showed that the two variants were Hb Broussais [alpha 90 (FG2)Lys-->Asn] and Hb Cemenelum [alpha 92 (FG4)Arg-->Trp].


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