64 



GERTRUDE E. PERLMANN 



TABLE III 



Rotatory Dispersion Constant, A,., and Specific Activity of Pepsin in Various 



Solvents as Function of Temperature 



Relative specific 

 Composition of solvent pH* Temperature A^ activity per unit 



nitrogen in per centf 



* Apparent pH. 



t The relative specific activity of a freshly prepared pepsin solution in o • i M 

 acetate buffer of pH 46 is taken as 100. 



230 



5*1: 225 



^^ 

 o o 



u O 



220 



• 0-In acetate 

 buffer 



- D 8-Om urea 

 A 5'Om guanidine 



hydrochloride \i 



-g---^n 



100 



80 



60 



40 



20 



20 30 40 50 



Temperature ( C) 



60 



Fig. 4. Dependence of temperature of the optical rotatory dispersion constant, 

 A,,, and enzymic activity of pepsin in various solvents. 



segment necessary for the biological activity of the enzyme has been 

 affected. 



From the results presented here, one can conclude : 



I. Although hydrogen bonds undoubtedly exist in pepsin, they are 

 relatively unimportant in maintaining the configuration of the protein 

 essential for its enzvmic action. 



