Study On Interaction Between Heavy Metal Ions And Arginine Kinase

Q SephroseTM-XL strong anion exchange chromatography was used to purifyshrimp arginine kinase from arginine kinase crude extract. The high purity of argininekinase had been proved by SDS-PAGE. Improve the pH of the activity of enzyme isdetermined by colorimetric method. Study on the properties of arginine kinase. Theeffect of heavy metal ions on catalytic activity and coagulation function of argininekinase. Study on the interaction between heavy metal ions and arginine kinase byfluorescence spectrum. The results show that arginine kinase is high purity、strongactivity, which is puritied by Q SephroseTM-XL strong anion exchangechromatography. With the increased concentration of heavy metals, the enzymeactivity gradually decline, the degree of coagulation enzymes to speed up. Thestronger the heavy metal ions of non-metallic, the greater the influence of enzymeactivity. According to the Stem-Volmer curve. The interaction between heavy metaland arginine kinase lead to arginine kinase fluorescent static quenching effect.According to the fomula of static quenching. With lg[(F0-F)/F] mapping of lg[c].Solved by the slope and intercept of Ag+with the combination of arginine kinaseconstant KA=3.881×105and numbers of combined with n=1.1968. Cu2+：KA=2.817×104numbers of combined with n=1.1055. Zn2+：KA=1.108×105andnumbers of combined with n=1.1943. Fe3+：KA=1.175×104and numbers of combinedwith n=1.0312. Cd2+：KA=1.538×104and numbers of combined with n=1.0021. Studyfully shows that different heavy metal ions influence mechanism of changes ofarginine kinase conformation and different levels. Study also proved that thefluorescence spectrum can sensitively reflect the arginine kinase molecularconformation change. Which is a good test of heavy metal ions that interact witharginine kinase tools.