The hydrolysis of N-benzoyl-L-argininamide by crystalline trypsin.
نویسندگان
چکیده
where e = the total enzyme concentration, s = the substrate concentration, t = the time, and K’ = the proteolytic coefficient (3) of the system. Reinvestigation of the above reaction over a greater range of initial substrate concentrations has now shown that the initial reaction velocity at 25’ is essentially independent of the initial substrate concentration for concentrations varying from 0.01 to 0.05 M and that, for these and lesser substrate concentrations, the initial reaction rates obey the MichaelisMenten (4) equation
منابع مشابه
The specific esterase activity of trypsin.
The discovery of relatively simple peptide derivatives as substrates for proteolytic enzymes has introduced a new approach to the problem of the specificity of this group of hydrolytic enzymes. Although crystalline trypsin is known to catalyze the hydrolysis of internal peptide bonds of proteins, its action toward internal peptide bondsof synthetic substrates has been demonstrated for only one ...
متن کاملSpecificity of chymotrypsin B.
Brown, Shupe, and Laskowski (1) have described the isolation, from beef pancreas, of a crystalline proteolytic enzyme which they have named “activated protein B” or “chymotrypsin B.” Through the kindness of Dr. Laskowski who provided us with a 4 times recrystallized sample of this enzyme, it was possible to examine its action on a series of synthetic peptides and peptide derivatives. The data p...
متن کاملThe Kinetics of the Amidase and Esterase Activities of Trypsin By
In previous reports from this laboratory investigations of the specific esterase activity of trypsin (1) and of the detailed kinetics of the hydrolysis of specific substrates by chymotrypsin and by carboxypeptidsse have been reported (2, 3). In the present paper a reinvestigation of the kinetics of the action of trypsin on benzoyl-L-argininamide and the results of kinetic studies of the action ...
متن کاملThe kinetics of the amidase and esterase activities of trypsin.
In previous reports from this laboratory investigations of the specific esterase activity of trypsin (1) and of the detailed kinetics of the hydrolysis of specific substrates by chymotrypsin and by carboxypeptidsse have been reported (2, 3). In the present paper a reinvestigation of the kinetics of the action of trypsin on benzoyl-L-argininamide and the results of kinetic studies of the action ...
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...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 178 2 شماره
صفحات -
تاریخ انتشار 1949