By A., ed. Meister
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 51
Enzymes of very high molecular weight cannot always be accommodated in micelles because of turbidity on the other hand, if one except enzymes with prosthetic groups or substrates strongly absorbing light, it is not possible to use the same concentrations used to carry out kinetic measurements by relaxation techniques. 3. ” Kinetic and thermodynamic parameters of a number of enzymecatalyzed reactions might be altered as compared to bulk water. Rate effects can result from electrostatic, hydrophobic interactions with the resultant alteration of the free energy of activation for the overall process.
Since the higher the water content, the higher the temperature at which micromicellar solutions become turbid, a compromise must be sought to accommodate the enzymes and to investigation them at subzero temperatures. 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.
Most of these solutions containing proteins are homogeneous, optically transparent down to 250 nm, and of low freezing point (I-50°C) but show turbidity well before this freezing point; the lowest temperature reached without appearance of turbidity was -4OOC with solutions of cytochrome c. Selected proteins appear to be soluble in reversed micelles depending largely on their molecular weight, water content, and, in fact, [water]/ [surfactant] ratio, but their absorption spectra are markedly influenced by this water-to-surfactant ratio.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 51 by A., ed. Meister