Nephelometric determination of elastase activity and method for elastoproteolytic measurements

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Abstract
It has been shown that the different methods in the literature for the measurement of elastase activity fail to give comparable results. One of the main reasons of this discrepancy lies in the fact that certain buffer salts inhibit elastolysis. This inhibition manifests itself differently with the different methods. With an ionic strength of 0. 1, which has been accepted in the literature, the pH-activity curves in different buffers fail to show the same optimum pH values; the inhibitory effect of the ions of the buffering salts is apparent when results with either similar or different methods are compared. A rapid and, within certain limits, sufficiently exact nephelometric method has been elaborated for the measurement of elastase activity. Conditions were examined under which the nephelometric and the Folin-phenol method can be combined to obtain good and reliable results in the determinations of pro-teolytic activity of elastase. In the course of nephelometric studies a new feature of elastase activity was revealed. The elastase increased the transparency of elastin particles in a concentration too low for its activity to be measured by the gravimetric or the Folin-phenol method.