روزنامه با شماره پیاپی سال 2002

5

147

151

The interaction of myelin basic protein (MBP) from bovine central nervous system with divalent copper ion was studied by equilibrium dialysis and isothermal titration calorimetry techniques at 27 °C in Tris buffer solution at pH=7.2. MBP has two binding sites for copper ion. The intrinsic association equilibrium constants are 0.083 and 1.740 μM−1 in the first and second binding sites, respectively. Hence, occupation of the first site has produced an appreciable enhancement 21 of the binding affinity of the second site. A new representation of titration calorimetric data, as well as, the Scatchard plot, shows positive cooperativity in two binding sites for copper ions. The molar enthalpies of binding are −13.5 and −14.8 kJ mol−1 in the first and second binding sites, respectively.

Food Microbiology

2002

Food Microbiology