Studies on Enzymatically Active Fragments of Pepsin
III. Further Purification and the Homogeneity of a Fragment with Peptic Activity
1962 年 52 巻 2 号 p. 103-107
詳細
1962 年 52 巻 2 号 p. 103-107
1. Further purification of the partially purified fragment of pepsin was attempted using a column of DEAE-cellulose and/or CM-cellulose and resulted in the separation of two components, a major enzymatically active component-Fragment A-and a minor inactive component.
2. Fragment A thus obtained behaved as a homogeneous protein ultracentrifugally, chromatographically, and electrophoretically.
3. Approximately one third of the total peptic activity produced in the dialysate by dialysis autolysis of pepsin (0.4 per cent of that of starting material) obtained in Frag-ment A and 1.7 per cent of total nitrogen produced in the dialysate (0.6 per cent of that of starting material) was obtained in Fragment A.
4. The specific activity of Fragment A against casein or bovine hemoglobin corresponded to approximately half of that of crys-talline pepsin.
We wish to express our thanks to Dr. Martin Sonenberg, Head, Metabolism Laboratory, Sloan-Kettering Institute for Cancer Research, for his help during preparation of the manuscript.
