By Felix Bronner and Arnost Kleinzeller (Eds.)

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I. BOGUSLAVSKY always arises when comparing the results of measuring the emf in the chain (30). and the potentials of chains (3 1) and (32), which are the halfcells of chain (30). Figure 5 shows the results of measuring the potentials in the chains that are analogous to chains (30)-(32). The salt, M X , is represented by (But),NCI, and nitrobenzene has been chosen for the oil phase. The emf of the water/nitrobenzene/water concentration chain in the presence of tetrabutylammonium chloride is significantly less then the sum of half-cell potentials measured in the chain by the vibrating electrode and radioactive probe technique.

The maximum enzymatic activity is therefore explained by the optimal orientation of substrate molecules at the given surface pressure. The conformational state of the enzyme seems to be also essential in this case, the enzyme being sensitive to the physical state of the substrate. The waterhir interface can be used to reconstruct the complexes containing more than two components. , 1970a,b). D. Galactosyltransferase at the AirlWater Interface The galactosyltransferase enzyme (IDP-galactose-lipopolysaccharide3-galactosyltransferase) belongs to membrane enzymatic systems, and is a catalyst for the transfer of galactose from IDP-galactose to the galactose-deficient lipopolysaccharide.

24 L. 1. BOGUSLAVSKY shows how the enzyme interacts with a previously formed mixed monolayer of phosphatidylethanolamine with galactose-deficient lipopolysaccharide. 164 mM of [3H]galactose. Control experiments conducted in the absence of one of the reaction components showed no appreciable incorporation of galactose into the monolayer. The rate of the reaction depends on divalent cations which accelerate the process. Magnesium was found to be the most effective cation. Ca2+and Mn2+ were significantly less effective.

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