Electrophoresis of pepsin

Electrophoresis of Pepsin

1. A number of pepsin solutions containing several protein components have been studied by the electrophoresis method. All samples show a homogeneous boundary moving to the anode at pH 4.4. 2. The activity of this material may be higher than that of the original solution on the basis of total nitrogen but is the same as that of the original solution on the basis of protein nitrogen. 3. There is...

Crystalline Pepsin Iii. Preparation of Active Crystalline Pepsin from Inactive Denatured Pepsin By

The results (1) of the experiments with crystalline pepsin isolated from crude pepsin preparations indicated that the material is a pure substance and that the proteolytic activity is a property of the protein molecule itself and is not due to the presence of a separate non-protein impurity. No indication of the presence of a more highly active nonprotein molecule was obtained in the solubility...

Crystalline Pepsin

The decrease in protein nitrogen and in the activity of solutions of crystalline pepsin at pH 1.8 and 45 degrees C. has been determined. The decrease in activity, as measured with eleven different methods, is in exact proportion to the decrease of protein nitrogen of the solution. The measurements were continued until less than 5 per cent of the original protein remained. These results indicate...

Transformation of Swine Pepsinogen into Swine Pepsin by Chicken Pepsin

Activation of swine pepsinogen with chicken pepsin results in the formation of swine pepsin. Activation of chicken pepsinogen with swine pepsin results in the formation of chicken pepsin. The structure responsible for the species specificity of the enzyme is therefore present in the inactive precursor.

The Specificity of Pepsin