منابع مشابه
Pepsinogen and Pepsin
Evidence relating to the structure and properties of swine pepsinogen and pepsin has been reviewed and used to suggest a tentative two dimensional picture of the skeleton of these two proteins. When pepsinogen, a folded single peptide chain, is converted to pepsin, there is a profound change in the physical and chemical properties of the protein. In an as yet unknown manner, except that it is i...
متن کاملBovine Pepsinogen and Pepsin
As the first step in the investigation of the structure and action of little known gastric zymogens and enzymes, pepsinogen has been isolated from the mucosa of the fourth stomach (abomasum) of the’ cow. The pepsinogen was purified by ammonium sulfate fractionation, batch absorption on diethylaminoethyl (DEAE) cellulose, recycling gel filtration on Sephadex G-100, and finally chromatography on ...
متن کاملPepsinogen and Pepsin
Evidence relating to the structure and properties of swine pepsinogen and pepsin has been reviewed and used to suggest a tentative two dimensional picture of the skeleton of these two proteins. When pepsinogen, a folded single peptide chain, is converted to pepsin, there is a profound change in the physical and chemical properties of the protein. In an as yet unknown manner, except that it is i...
متن کاملPepsin from Pepsinogen
Commercial samples of crystalline swine pepsin have been found to be heterogeneous by a number of criteria. Several active fractions can be obtained by chromatography on hydroxylapatite with phosphate buffers, pH 5.7, of increasing molarity as eluents. This has been found to be an effective procedure for evaluating the homogeneity of pepsin. End group analysis by the cyanate method yields 1 eq ...
متن کاملEnzymic Dephosphorylation of Pepsin and Pepsinogen
It has been shown by the work presented in this paper that it is possible to dephosphorylate enzymically pepsin and pepsinogen with a variety of phosphatases. With the aid of a phosphodiesterase and the prostate phosphatase it has been established that the phosphorus in the two proteins is present as a diester and connects two sites of the peptide chain in a cyclic configuration. Removal of the...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)34178-x