Investigation of the Aging Processes in Rubber. I. The Effect of Irradiation with Ultra-violet Light or the Surface Tension of Rubber Solutions

1934 ◽  
Vol 7 (2) ◽  
pp. 302-308
Author(s):  
B. Dogadkin ◽  
G. Pantschenkow

Abstract 1. Irradiation of rubber solutions in the presence of air with ultra-violet light brings about a pronounced lowering of their surface tensions at the boundary of solution and water. This lowering is connected with the formation of oxidation products of rubber, which are surface-active. 2. The kinetics of the changes in the surface tension are similar to those of the changes in viscosity brought about by irradiation of the solutions. 3. Irradiation of solutions of purified rubber in an atmosphere of nitrogen does not bring about any change in their surface tensions, as judged by the values of the minima of their isotherms. 4. These facts show that, in the absence of oxygen, light may exert an independent effect on rubber by causing depolarization of the rubber molecules and disaggregation of the micelles, which is closely related to this depolarization. In a general way, the nature of the action of light on rubber and the conditions necessary for the light to be effective are explained by the present work. In conclusion, the authors wish to express their appreciation to Professor A. A. Seide for his kindness in furnishing the samples necessary for the work.

1920 ◽  
Vol 3 (2) ◽  
pp. 185-201
Author(s):  
S. C. Brooks

It has been shown: 1. That complement exposed to ultra-violet light is not thereby sensitized to the action of heat (which indicates that it is not protein). 2. That inactivation of complement by ultra-violet light is accompanied by a decrease in its surface tension. 3. That photoinactivation of complement is not a result of any changes in hydrogen ion concentration since these are less than 0.05 pH. 4. That hydrogen ion concentrations high enough to transform serum proteins from the cation to the anion condition (i.e. past the isoelectric point) permanently inactivate complement. These facts together with those given in previous papers lead to the following hypotheses. 1. That there is present in serum a hemolytic substance which is formed from a precursor (which may resemble lecithin) and is constantly being formed and simultaneously being broken down into inactive products. 2. That both precursor and lysin contain the same photosensitive molecular group. 3. That the lytic substance is dependent for its activity upon the state of the serum proteins.


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