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Each type of enzyme needs to be examined individually to determine medium conditions ensuring both its normal spectral response and its investigation at a suitable range of subzero temperatures. Figure 21 shows absorption spectra of horse radish peroxydase at two temperatures in an homogeneous micellar solution. It can be seen that decreasing temperature determines the usual sharpening of absorption bands and increasing diffusion. With other proteins such as cytochrome c , slight variations of Amax (blue shift) have been CRYOENZYMOLOGY IN AQUEOUS MEDIA 45 Fig.

The surfactant shell may be a locus of solubilization, as well as the hexagonal packing of the water cylinder. Last, the solubilization sites are not fixed and some spectral changes recorded upon changing temperature conditions might be due to shifts in equilibrium among different possible sites. Since a large variety of phases can exist in equilibrium with each other, each phase might provide quite different environments for protein molecules. Present lack of deeper analysis and data requires systematic empirical assays for each solubilized enzyme and no general conclusion can be drawn from individual behaviors.

5 kcal M - ' , both values being very close to those of Gibson. Significant differences were observed when the reaction was carried out in a methanol-buffer system. While the activation energy calculated from experiments carried out from -55 to -1 1"C is about the same as that in an ethylene glycol -buffer system, the absolute value of the rate constants for a given temperature are quite different, lower by about one order of magnitude. 4 X 10' M-' sec-', which is similar to the value reported in methanol-water mixtures.

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