Studies of the binding of alpha-lactalbumin to immobilized peptide ligands.
The present work investigates the mechanism of binding of alpha-lactalbumin to the peptide ligand WHWRKR and its variants HWRKR and acetylated WHWRKR immobilized on a polymethacrylate chromatographic resin. The presence of two temperature-dependent binding mechanisms and one temperature-independent mechanism was demonstrated. Injections of different forms of alpha-lactalbumin (apo-alpha-lactalbumin, D87A mutant alpha-lactalbumin) displayed similar behaviors when compared to native alpha-lactalbumin, while lysozyme showed little or no binding to the WHWRKR and AcWHWRKR resins. An alternative process for isolation of alpha-lactalbumin from WPI was shown, using consecutive injections of WPI with limited elution.
Gurgel
P V
PV
Department of Food Science, Box 7624, North Carolina State University, Raleigh, North Carolina 27695-7624, USA.
Carbonell
R G
RG
Swaisgood
H E
HE
D000327:Adsorption; D000595:Amino Acid Sequence; D007768:Lactalbumin / Q000378:metabolism*; D008024:Ligands; D016297:Mutagenesis, Site-Directed; D009842:Oligopeptides / Q000378:metabolism*; D011485:Protein Binding; D011498:Protein Precursors / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D012116:Resins, Plant; D013816:Thermodynamics
D008024:Ligands; D009842:Oligopeptides; D011498:Protein Precursors; D011994:Recombinant Proteins; D012116:Resins, Plant; D007768:Lactalbumin