Crystalline Pepsin
نویسنده
چکیده
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 that none of the split products of the protein molecule possess any appreciable activity compared to that of the original protein.
منابع مشابه
The Presence of a Gelatin-liquefying Enzyme in Crude Pepsin Preparations
A protein fraction has been isolated from crude pepsin preparations which is about 400 times as active as crystalline pepsin in the lique-faction of gelatin. The activity as measured by the digestion of casein, edestin or egg albumin is less than that of crystalline pepsin. It is more resistant to alkali than the crystalline pepsin.
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IN a recent series of publications Northrop [1930, 1, 2; 1931] has advanced very strong evidence that pepsin is a protein. Starting from commercial pepsin, by suitably regulating the pH and precipitating with the aid of magnesium or ammonium sulphate a crystalline product was obtained which had the general properties of a protein. In particular, solutions of this crystalline pepsin were coagula...
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ورودعنوان ژورنال:
- The Journal of General Physiology
دوره 13 شماره
صفحات -
تاریخ انتشار 2003