THE RELATION OF PROTEOLYTIC ENZYMES IN THE PNEUMONIC LUNG TO HYDROGEN ION CONCENTRATION. AN EXPLANATION OF RESOLUTION

Abstract

Evidence is given of the presence in the cellular material obtained from the pneumonic lung of a proteolytic enzyme digesting coagulated blood serum at hydrogen ion concentrations of 7.3 to 6.7 and inactive at higher; i.e., more acid concentrations. In addition, evidence is brought forward of the presence in the cellular material from the pneumonic lung of a proteolytic enzyme splitting peptone to amino-acid nitrogen. This enzyme is operative at hydrogen ion concentrations from 8.0 to 4.8, but most active at 6.3 or 5.2. These findings may be regarded as having a bearing on resolution in pneumonia. During the course of the disease a gradual increase in the hydrogen ion concentration of the exudate probably takes place. With the breaking down of cellular material an enzyme digesting protein (fibrin) in weakly alkaline and weakly acid media may be liberated. With a gradual increase in the hydrogen ion concentration of the pneumonic lung the action of this enzyme probably ceases. An enzyme capable of splitting peptone to amino-acid nitrogen is probably active during the proteolysis of the fibrin and further activated when the hydrogen ion concentration of the pneumonic lung is increased to within its range of optimum activity at a pH of 6.3 and 5.2. By this means it may be conceived that the exudate is dissolved and resolution takes place.