Purification of hemoglobin, myoglobine and sytocrom-c proteins in the blood serum by using lantanide containing molecular imprinted cryogel polymers

Hemoglobin analysis is particularlyimportant in thediagnosis of anemicdiseases, in thattheanalysis of myoglobinanalysis is particularlyimportant in thediagnosis of heartattacks, muscle-tissueandkidneydisorders, and in cytochrome-C analysis it is thoughtto be used in bloodformationandquantification of ions in celltissues.Inthisstudy, hemoglobin (Hb), myoglobin (Mb) andcytochrome-C (Sit-C) proteins in aqueoussolutionandblood serum weredetected in the presence of variousproteinsusing a newlanthanide-containingpolymer, p-HEMA-MAAP- aqueoussolutionsandwithhighselectivityfromthebloodserum.The protein imprintedpolymersusedforthispurposewaspreparedbythefreeradicalpolymerisationmethod.MAAP (methacryoylamidoantipyrine) wasused as thefunctionalmonomerand MAAP-Ce(III) complexmonomerswerecomplexedwiththe Ce(III) ionfromthelanthanidegroupelementscapable of coordinationbond in highnumber in ordertoincreasethebindingactivity.Theprepared MAAP-Ce(III) complexmonomer, p-HEMA (poly-2-hydroxyethylmethacrylate) andtheindividualcuredproteinswerepreparedbyinteractionwitheach protein andthentherepressedproteins in thepolymerweredesorbedwith0.1 M NaCl-Na2SO4, Hb, Mband Sit-C imprintedlanthanide-containing p-HEMA-MAAP-Ce(III) cryogelpolymerswereprepared.Characterization of thepreparedcomplexmonomers, imprintedandnonimprintedpolymerswereperformedby FT-IR, Near-IR and SEM. Parameterssuch as pH, flow rate, initial protein concentration, salt effect, number of reproducibilitywereinvestigatedandoptimumconditionsweredetermined in experimentstodetermine optimum conditions in bindingstudies.It has beenfoundthattheimprintedpolymers (MIP) preparedunderoptimumconditionshave a highselectivityandbindingactivitycomparedtothenonimprintedpolymers (NIP).Furthermore, in thedeterminedoptimumconditions, thebindingactivities of theproteinsmentioned in theblood serum of thepreparedimprintedpolymerswereexaminedandfoundto be highlyselectiveagainstthetargetproteins.