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

2004 Bulletin of the Korean Chemical Society (Print)  
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 (BS 3 ), N-hydroxysuccinimide 3-(2-pyridyldithio)propionate (SPDP), or N-hydroxysuccinimide 4maleimidobutyrate (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
more » ... ulfide 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.
doi:10.5012/bkcs.2004.25.9.1366 fatcat:kxtlejlsbbhq7d5b4mvncqxtme