Protein Complexes as Biochemically Active Systems 



183 



1-1 



1-0 

 0-9 

 0-8 

 0-7 

 0-6 

 0-5 



!4oo V^oo Moo 



'/so 



K25 



Fig. 2. The digestion of serum albumin by trypsin (I) and by the trypsin-ergosterol 

 complex (II) as a function of the amount of enzyme (see text). 



density at zero time. These data are in accord with the experimental results in 

 Fig. 2, On the basis of these data we selected an enzyme/substrate ratio lying 

 between 1/50-1/100 to study the kinetics of proteolysis of serum albumin by 

 trypsin-ergosterol complex. 



0-5 



hr 



Fig. 3. The kinetic curves for serum albumin proteolysis by trypsin (I) and by 

 its complex with ergosterol (II) obtained spectrophotometrically. 



Fig. 3 gives the kinetic curves for serum albumin proteolysis by trypsin (curve 

 I) and by its complex with ergosterol (curve II); the curves are obtained spectro- 

 photometrically. Fig. 4 gives similar curves representing the rates of increase 

 of amino N, as determined by the method of Van Slyke. 



Here the volumetric readings in ml N2 are plotted against the time in hours. 

 From the data of Fig. 3 and Fig. 4 it follows that the formation of the complex 

 appreciably increases the proteolytic activity of the enzyme and the degree of 



