Growth of Clostridium pasteurianurn was inhibited in media of high solute content. At equal osmolarities, 'permeant' solutes (glycerol and acetamide) were much less growth-inhibitory than 'non-permeant' solutes (KC1 and xylitol). Glycolysis by washed cell suspensions was inhibited by these solutes in parallel with growth. However, in their inhibition of glucose 6-phosphate dissimilation by permeabilized cells the distinction between 'permeant' and 'impermeant' solutes was significantly less marked. The glucose phosphotransferase system (PTS) of intact cells was much more strongly inhibited by 'non-permeant' than by 'permeant' solutes. It was concluded that the predominant inhibitory effects on this organism of media of high solute content are due not to the low water activity of such media per se, but to the creation of an osmotic pressure across the bacterial cytoplasmic membrane, which acts to inhibit the glucose PTS by which the organism effects glucose uptake. Parallel measurements of the effects of xylitol on both glycolysis and the activity of the glucose PTS suggested that despite this correlation between the osmotic inhibition of growth, glycolysis and the PTS, the flux-control coefficient of the PTS on glycolysis did not exceed 0.2 under the conditions used.
A supported liquid membrane system was investigated for the carrier mediated transport of phenylalanine to more fully understand the contradictory effects, described in the literature, of chloride ion concentration in the aqueous phases on the stability of the system. The role of the organic phase and its interaction with carrier and support material was considered. The carrier mediated transport was comparable to an enzyme mediated process. Kinetic studies were undertaken and the data interpreted in a manner appropriate to biological transport processes to consider the transport process at a molecular level. The system was shown to deviate from a direct 1: 1 exchange process between phenylalanine and chloride and had a high degree of selectivity with respect to phenylalanine.
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