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Effect of Linker for Immobilization of Glutathione on BSA-Assembled Controlled Pore Glass Beads



Controlled pore glass bead was modified with bovine serum albumin (BSA), and glutathione (GSH) was immobilized through three kinds of linkers on top of BSA. Bis(3-sulfo-N-hydroxysuccinimide suberate) sodium salt (BS3), N-hydroxysuccinimide 3-(2-pyridyldithio)propionate (SPDP), or N-hydroxysuccinimide 4-maleimidobutyrate (GMBS) was introduced into the BSA-bound matrix. Subsequently, GSH was immobilized by addition of thiol side chain into the maleimido moiety, replacing a disulfide group, or formation of an amide group upon releasing 3-sulfo-N-hydroxysuccimide group. It was observed that conjugation methodology
played a critical role for activity of the immobilized GSH. SDS-PAGE chromatogram showed that the matrix of glutathione immobilized on BSA through GMBS manifested high selectivity towards glutathione-Stransferase (GST) in cell lysate.

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http://www.namipan.com/d/f6cb83d ... 551e06d004cdadf1200


Interaction of Sucrose Esters with Skim Milk Proteins as Characterized by Affinity Chromatography

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http://www.namipan.com/d/a093535 ... ed0ba3658322a2e0900

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