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The low value for cyclohexane is more difficult to explain (no value for cho lesterol solubility in cyc lohexane was obtained); one could argue that cyc l ohexane has a structure somewhat similar to that of the reactive end of the substrate molecule that binds to the active site, and therefore could be responsible for inhibition of the enzyme reaction . Another factor to bear in mind is the stability of the enzyme in the presence of interfaces in the heterogeneous system. "lIIDObilization" in the cells in reaction system A may afford some protection, whereas in reaction system B this effect is probably achieved by the addition of serum albumin to the system (Cremonesi et al .

The problem always remains of defining the degree of immiscibility. In any case a balance between activity and stability must be considered as exemplified in experiments by Buckland et al. (1975) and Cremonesi et al. (1975), summarized in Table 2. In the case of reaction B, having NAD as a co-factor, the less the solvent is soluble in water the higher is the enzyme activity (not shown in the table). Carbon tetrachloride seems to support an enzyme activity higher than predicted by its solubility in water when compared with chlorobenzene.

Martinek, K. , 1977, Biotechnol. , 19:1351. , Samokhin, G. , 1978, Bioorganicheskaya Khimiya, 4:82. , 1965, Faraday Soc. Discussions, 20:83. Laidler, K. , 1973, "The Chemical Kinetics of Enzyme Action", 2nd edition, Clarendon Press, Oxford. , Ryan, F. , 1974, Adv. Exp. Med. , 42:259. , Brusca, D. , 29 July 1979, US Patent 3,897,308. Llor, J. , 1977, J. Chem. Soc. , 11:1111. , Casellato, M. , 1973, Arch. Biochem. , 159:1. , Klyachko, N. , 1977, Doklady Akademii Nauk SSSR, 236:920. , 1978, J. BioI.

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