STUDIES ON THE TRYPSINOGEN, ENTEROKINASE, AND TRYPSIN SYSTEM
نویسندگان
چکیده
منابع مشابه
Formation of Trypsin from Crystalline Trypsinogen by Means of Enterokinase
Crystalline trypsinogen is most readily and completely transformed into trypsin by means of enterokinase in the range of pH 5.2-6.0 at 5 degrees C. and at a concentration of trypsinogen of not more than 0.1 mg. per ml. The action of enterokinase under these conditions is that of a typical enzyme. The process follows closely the course of a catalytic unimolecular reaction, the rate of formation ...
متن کاملCrystalline Chymo-trypsin and Chymo-trypsinogen
A new crystalline protein, chymo-trypsinogen, has been isolated from acid extracts of fresh cattle pancreas. This protein is not an enzyme but is transformed by minute amounts of trypsin into an active proteolytic enzyme called chymo-trypsin. The chymo-trypsin has also been obtained in crystalline form. The chymo-trypsinogen cannot be activated by enterokinase, pepsin, inactive trypsin, or calc...
متن کاملIsolation from Beef Pancreas of Crystalline Trypsinogen, Trypsin, a Trypsin Inhibitor, and an Inhibitor-trypsin Compound
Methods are described for the isolation and crystallization of trypsinogen, trypsin, a substance which inhibits trypsin, and an inhibitor-trypsin compound. Analyses and some of the properties of these compounds are given.
متن کاملStudies on the autocatalytic activation of trypsinogen.
Recent work on the autocatalytic conversion of trypsinogen to trypsin (1, 2), first described by Kunitz and Northrop (3), has brought to focus a more detailed picture of the chemical changes accompanying this transformation. Thus, it has been shown that during the activation, and simultaneously with the appearance of tryptic activity, a lysyl-isoleucine bond is broken in the N-terminal region o...
متن کاملHydrolysis of artificial substrates by enterokinase and trypsin and the development of a sensitive specific assay for enterokinase in serum.
The activities of highly purified human enterokinase (enteropeptidase, EC 3.4.21.9) and bovine trypsin were tested against three synthetic substrates alpha-N-Benzoyl-L-arginine ethyl ester HCl, alpha-N-Benzoyl-DL-arginine-p-nitroanilide HCl and alpha-N-Benzoyl-DL-arginine-2-naphthylamide HCl. There was no detectable hydrolysis of these substrates by enterokinase whereas the kinetic parameters o...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1935
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)75080-1