earticle

영어

Recombinant human H- and L-ferritins(FNs) were purified from Saccharomyces cerevisiae and characterized. Molecular properties were examined with respect to its electrophoretic mobility, isoelectric point (pI), iron uptake kinetics and reconstitution yield of the ferritin core. On SDS-PAGE, the yeast-derived FNs showed bands with the similar mobilities to the corresponding E. coli-derived ones. The pI pattern of yeast-derived H-FN was relatively comparable to that of E.
coli-derived while pI of L-FN was more acidic than that of E. coliderived. The recombinant H- and L-FNs are non-glycosylated as proven by cells treated with tunicamycin. To confirm whether the recombinant FNs were phosphorylated, Western blot was performed using antibodies for Ser, Thr and Tyr. The H-FN was determined to be phosphorylated at Ser and Tyr sites while L-FN was not at all. Decrease in the initial rate of the iron uptake kinetics may be caused by such phosphorylation as the residues of Ser and Tyr are known to be closely related to the ferroxidase sites of this protein. In addition, the H-FN exhibited the highest reconstitution yield among the FNs examined, which means it is advantageous to the formation of the
inorganic nano particles using the protein.