scholarly journals Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography

PROTEOMICS ◽  
2008 ◽  
Vol 8 (7) ◽  
pp. 1346-1361 ◽  
Author(s):  
Guanghui Han ◽  
Mingliang Ye ◽  
Houjiang Zhou ◽  
Xinning Jiang ◽  
Shun Feng ◽  
...  
Keyword(s):  
Anion Exchange ◽  
Liver Tissue ◽  
Human Liver ◽  
Large Scale ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Human Liver Tissue ◽  
Strong Anion Exchange

Highly substituted BHAR:Synthesis and application for large scale SPPS and for anion exchange chromatography

Peptides ◽  
1994 ◽  
pp. 252-253 ◽  
Author(s):  
A. Etchegaray ◽  
R.S.H. Carvalho ◽  
R. Marchetto ◽  
C.R. Nakaie
Keyword(s):  
Anion Exchange ◽  
Large Scale ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography

Separation of acidic protein tyrosine kinase substrates by strong anion-exchange chromatography

1998 ◽  
Vol 813 (2) ◽  
pp. 277-283 ◽  
Author(s):  
P Ruzza ◽  
A Calderan ◽  
B Biondi ◽  
B Ancona ◽  
G Borin
Keyword(s):  
Tyrosine Kinase ◽  
Anion Exchange ◽  
Protein Tyrosine Kinase ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Acidic Protein ◽  
Protein Tyrosine ◽  
Strong Anion Exchange ◽  
Kinase Substrates

Separation of bovine κ-casein glycomacropeptide from sweet whey protein products with undetectable level of phenylalanine by protein precipitation followed by anion exchange chromatography

2018 ◽  
Vol 85 (1) ◽  
pp. 110-113 ◽  
Author(s):  
Takuo Nakano ◽  
Lech Ozimek ◽  
Mirko Betti
Keyword(s):  
Heat Treatment ◽  
Amino Acid ◽  
Whey Protein ◽  
Anion Exchange ◽  
Large Scale ◽  
Dry Weight ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Ph Shift ◽  
Sweet Whey

Bovine κ-casein glycomacropeptide (GMP) found in sweet whey is a 64 amino acid residue glycopeptide, which does not contain phenylalanine or other aromatic amino acids. There is, however, little information available concerning isolation of phenylalanine free GMP from sweet whey. In the study reported in this Research Communication, GMP was purified from three samples of sweet whey protein products (SWPP) by a procedure involving: (1) precipitation of protein by heat treatment; (2) precipitation of protein by pH shift to 4·6; and (3) diethylaminoethyl (DEAE)-Sephacel anion exchange chromatography of soluble portion of each sample obtained after removal of protein precipitates. The total protein precipitated with both heat treatment and pH shift accounted for average 61% of dry weight of SWPP. The GMP fraction obtained by DEAE-Sephacel chromatography accounted for average 7·5% of dry weight of SWPP. Amino acid analysis showed that there was no detectable level of phenylalanine in GMP fractions from all samples examined. The present method may help develop large scale methods of production of GMP.

scholarly journals Heparin Isomeric Oligosaccharide Separation Using Volatile Salt Strong Anion Exchange Chromatography

2016 ◽  
Vol 88 (23) ◽  
pp. 11542-11550 ◽  
Author(s):  
Rebecca L. Miller ◽  
Scott E. Guimond ◽  
Maitreyi Shivkumar ◽  
Jemma Blocksidge ◽  
James A. Austin ◽  
...  
Keyword(s):  
Anion Exchange ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Strong Anion Exchange

Efficient and easily scalable protein folding strong anion exchange chromatography for renaturation and simultaneous purification of recombinant human asparaginase from E. coli

2018 ◽  
Vol 34 (4) ◽  
pp. 1036-1044 ◽  
Author(s):  
Rajesh Kumar Kante ◽  
Sandeep Vemula ◽  
Maheswara Reddy Mallu ◽  
Srinivasa Reddy Ronda
Keyword(s):  
Protein Folding ◽  
Anion Exchange ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
E Coli ◽  
Strong Anion Exchange
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