Hydrophobic interaction of extracellular protein A from Staphylococcus aureus with octyl-sepharose CL-4B.
Extracellular Protein A from Staphylococcus aureus was shown to bind to alkyl agarose adsorbents of different carbon chain length. Octyl-Sepharose CL-4B was chosen to purify the active material, as the strong interaction with this adsorbent allowed the separation of Protein A from the bulk of the contaminants. Protein A retained its ability to bind to IgG in the presence of up to 3.5 M ethylene glycol as demonstrated by hemagglutination. A theory on the possible involvement of hydrophobic interaction in the binding reaction of Protein A to IgG is advanced.
D006386:Hemagglutination Tests; D007122:Immunoelectrophoresis; D012685:Sepharose / Q000031:analogs & derivatives; D013205:Staphylococcal Protein A / Q000302:isolation & purification*; D013211:Staphylococcus aureus
D013205:Staphylococcal Protein A; C027176:octyl-sepharose CL-4B; D012685:Sepharose