Title : Thermally-modulated on/off-adsorption materials for pharmaceutical protein purification.

Pub. Date : 2011 Jan

PMID : 20888041






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Chromatograms of two proteins indicated that negatively-charged HSA was adsorbed on the cationic copolymer brush modified silica beads at higher temperatures with low concentration of phosphate buffer (PB) (pH 7.0) as a mobile phase. copolymer albumin Homo sapiens
2 The HSA adsorption was attributed to (1) an enhanced electrostatic interaction with the cationic copolymer brush at low concentration of PB and (2) an increased hydrophobic interaction from the dehydrated copolymer at high temperature. copolymer albumin Homo sapiens
3 Step-temperature gradient enabled HSA and gamma-globulin to be separated by the modulation of HSA adsorption/desorption onto the copolymer brush grafted silica beads. copolymer albumin Homo sapiens
4 Step-temperature gradient enabled HSA and gamma-globulin to be separated by the modulation of HSA adsorption/desorption onto the copolymer brush grafted silica beads. copolymer albumin Homo sapiens