By Bennett R., Bowers R. G.
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Extra info for A baseline model for the co-evolution of hosts and pathogens
4, even the stabilization of the free SH moieties using iodo-acetamide could not prevent this uncontrolled recombination. It was most attractive to assign the recombination of these alkylated monomers to electrostatic forces and/or hydrogen bonding. This thought was substantiated by heating the aggregated dimers in 4 M urea for 3 min to 95 °, followed by rapid cooling in an ice bath. Surprisingly, monomers were obtained which remained stable for several days (797). In contrast to the native blue erythrocuprein, the monomeric Cu protein was colourless although it was EPR-active.
T e t r a b u t y l - a m m o n i u m superoxide was found convenient for the superoxide dismutase assay since it dissolved readily without decomposition in N,N-dimethyl formamide (70). Infusions of this solution into a cuvette containing aqueous oxidized cytochrome c reduced the available cytochrome c. In the presence of different erythrocuprein concentrations the reduction rate was progressively diminished. According to McCord and Fridovich (70) an enzyme unit was defined as 50% inhibition of the rate of reduction of cytochrome c.
It was interesting to note that the fine structure of the UV absorption spectra of apoerythrocuprein and the Zn protein remained essentially constant (72, 78, 722). This was not the case if Cu 2+ was employed. One Cu 2+ alone was able to produce both a profound increase of absorption and a change in the absorption profile (72, 78). In fact, the 2 Cu apoprotein displayed almost the same characteristics as the fully reconstituted protein although ~,max was shifted in all cases some 50 nm to lower wavelengths.