E. ACKERMAN, G. K. STROTHER AND R. L. BERGER 



31 



using the powdered catalase. However, with the crystallized catalase k/ 

 also varied with the fluidity. This variation is similar to that predicted 

 from the 405 iu/a results using either the powdered or crystallized catalase. 



.55- 



.50- 



.45 

 .♦0 

 .35 

 .30 

 .2S 

 .20 



wotar 

 — © 



^0 



1.5 

 1.0 

 .5 



1 10^ lll*ri/mel* iic 

 k,' 



cr 



J. 



pois* 



10 



20 30 40 50 60 70 60 90 



Fig. 4. Variation of ki' and Pi/e with fluidity. 



100 



110 



ANALYSIS AND DISCUSSION 



The variations of ki' and p/e with temperature were used to compute 

 values of ki and k4 . These are shown in figure 5. Similar lines, but with 

 a greater spread, can be derived from the data of 405 m/^. 



The extreme flatness of the ki curve is surprising; this constant is ap- 

 parently unaltered by temperature changes. Interpreting ki on the basis 

 of absolute rate theory, one finds that the free energy of activation is 

 purely an entropy. This entropy must have a large negative value, and 

 may correspond to the reduction in the disorder of the system upon the 

 formation of the intermediate complex, p (7). 



The heat of activation for k4 is greater than that for the fluidity of 

 water. This may be due to differences between the temperature dependence 

 of the fluidity of HoO and diffusion rate of HoOo . 



Tlie complex dependence of the diffusion rate constant, Di , on fluidity, 

 r)~^, as illustrated in figure 6, is reproduced from another paper (4). The 

 constant of interest to us here is Dfick for O2 in glycerol solutions. The 

 initial rise of D as ?/ is raised from that of water is surprising. If k4 is dif- 

 fusion dependent, and if the diffusion rate, D, is the same for both O2 and 



