Dilatometric, refractometric and viscometric study of lysozyme-cation interaction.
The interaction between hen egg-white lysozyme and Cu(II) or Co(II) cations has been studied by dilatometry, equilibrium dialysis-differential refractometry and viscometry at different metal cation concentrations. Delta V isotherms in copper and cobalt solutions have been obtained from dilatometry. Preferential adsorption parameters and specific viscosity have been determined from refractometric and viscosimetric measurements. It has been observed that this interaction produces structural alterations in lysozyme. The magnitude of these conformational changes depends on the metal ion and protein concentration. The results obtained using the three techniques are in good agreement.
D000818:Animals; D001665:Binding Sites; D002413:Cations, Divalent; D002645:Chickens; D003035:Cobalt; D004529:Egg White; D007700:Kinetics; D009113:Muramidase / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D014783:Viscosity
D002413:Cations, Divalent; D003035:Cobalt; D009113:Muramidase