Biochemical Processes in the Simplest Structures 



431 



enzyme was expressed in terms of ml. o-oi N-KMn04 consumed for titration 

 of the remaining hydrogen peroxide. Simultaneous control determinations were 

 made on samples with inactivated enzyme. The catalase of the lysate was in- 

 activated in the autoclave at i atm. for 30 minutes. 



In this way we determined the total catalase activity of the whole coacervate, 

 consisting of coacervate drops and the surrounding equilibrium fluid. 



To decide the question as to how the enzyme was distributed between the 

 coacervate drops and the equilibrium fluid, we prepared two coacervates, 'A' 

 and 'B', Coacervate 'A' contained the active enzyme, while coacervate 'B' 

 contained inactivated enzyme. Both coacervates were kept without H2O2 for 

 three minutes at a temperature of + 41-43 ''C and then centrifuged in the cold. 

 The supernatant of coacervate 'B' was added to the sediment of coacervate 'A', 

 while the sediment of coacervate 'B' was added to the equilibrium fluid (super- 

 natant) of coacervate 'A'. 



Thus, the first system corresponded to the coacervate drops of the coacervate 

 containing the active enzyme, and the second system to the equilibrium fluid of 

 that same coacervate. 



These mixtures were placed in a thermostat at 41-43 °C for three minutes; 

 then hydrogen peroxide was added to them and the activity of the enzyme was 

 determined in the manner described above. 



The results of the experiments are shown in Table 2. 



Table 2 

 Determination of the activity of catalase in coacervates 



The figures given above show that the catalase activity of the bacterial lysate 

 is concentrated entirely in the coacervate drops, while there is practically no 

 enzyme in the equilibrium fluid. 



The second method of investigation suggested by us was applied in studies 

 carried out in collaboration with N. Gel'man and I. Zhukova. Methods recently 

 developed for the isolation of separate structural elements of the cell have made 

 possible the study of the connection between the structure of the cell and the 

 processes taking place within it. In our experiments we made use of the fact that 

 by treatment of the cells of Micrococcus lysodeikticus with lysozyme in the 

 presence of different concentrations of sucrose, fragments of bacterial cells — 

 protoplasts — can be obtained with a greater or lesser degree of destruction of the 



