Implication of Methods and Techniques of Relaxation for Investigating the Iron release mechanism of Transferrin

Abstract

Transferrins (Tfs, serum transferring (sTf), ovotransferrin (oTf), lactotransferrin(Lf)) are bilobal iron binding glycoprotein's. In the absence of iron, the two lobs are in open conformation. Upon complex formation with iron and the protein is transformed to closed conformation and each lobs forms interdomains hydrogen bond and these are different from one transferrin to other. More over iron release from sTf and oTf take places in mildly acidic media while Lf releases iron in acidic conditions. This difference is likely due to proton assisted di-lysines triggers present in N-lobe of sTF and oTF but absent in Lf. This difference also reflected in kinetic and mechanism of iron release from TFs under mildly acidic pH conditions in the presence of physiological anions. This project discussing the implication of methods and techniques of relaxation for investigating the kinetics and mechanisms of iron release from Tfs' The comparison in kinetic and mechanistic steps of iron release from diferric-sTf, oTf and Lf showed that under mildly acidic conditions, the iron release from diferric-sTf and oTf occur in multiphasic manner while in diferric-sTf it occur it single phase