When thalidomide was immobilized on FG beads and affinity purification was performed from human cell extract, cereblon (CRBN) and DDB1 were identified. Cereblon is a constituent of an enzyme involved in protein degradation, and thalidomide has been found to cause teratogenicity by inhibiting the action of this enzyme.
Reference:T. Ito et al., Science 327 (2010) 1345
When a capsaicin derivative (Cap-NH2) was immobilized on FG beads and affinity purification was performed from human leukemia NB4 cells, Prohibitin1 and Prohibitin2 were identified. From this result the mechanism was elucidated by which capsaicin induces apoptosis in leukemia cells.
Reference:C. Kuramori et al., Biochem. Biophys. Res. Commun. 379 (2009) 519
The immobilization site of MTX was changed and immobilized on FG beads. Each target protein was subject to affinity purification from cancer cell extract. The target proteins DHFR (dihydrofolate reductase) and dCK (deoxycytidine kinase) were purified by different immobilization sites. From this result the mechanism of anticancer action of MTX was elucidated in detail.
Reference:H. Uga et al., Mol. Pharmacol. 70 (2006) 1832
The EspB protein of pathogenic Escherichia coli was immobilized on the beads, and the affinity was purified from the human cell extract. It could be confirmed that the EspB protein to bind to Myosin1C and inhibit its function.
Reference:Y. Iizumi et al., Cell Host & Microbe. 2 (2007) 383
For other examples, see
PAGE TOP
