The preparation and purification of individual human pepsins by using diethylaminoethyl-cellulose.
نویسندگان
چکیده
A procedure was devised for isolating human pepsins 1, 2, 3 and 5 from gastric juice by repetitive column chromatography on DEAE-cellulose. The combined yields in four different experiments varied from 14% to 90% of the total peptic activity of the starting material. The isolated individual pepsins were shown to behave as single homogeneous proteins on agar-gel electrophoresis at pH 5.0 and on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. There is preliminary evidence, requiring further study, of two other pepsins, one migrating between pepsins 1 and 2 and the other a pepsin-3 component associating closely with pepsin 5 on chromatography.
منابع مشابه
Studies on transfer RNA-Phe from Morris 5123C hepatoma.
its purification a benzoylated diethylaminoethyl cellulose column (7), after which we passed the preacylated tRNAsi^c: over an RPC-II column. This last column is described in Chart 1. The Chromatographie profile of the phenylalanine acceptor activity presented 3 distinct peaks. Those indicated as Phe 1 and Phe 2 were also normally present in tRNAs^a 0); Phe X is a new tRNA that we first observe...
متن کاملGlucose 6-phosphate dehydrogenase of human erythrocytes. I. Purification and characterization of normal (B+) enzyme.
Human erythrocyte glucose 6-phosphate dehydrogenase (o-glucose 6-phosphate :nicotinamide adenine dinucleotide phosphate oxidoreductase, EC 1.1.1.49) was purified by column chromatography with diethylaminoethyl cellulose, calcium phosphate gel, carboxymethyl cellulose, diethylaminoethyl Sephadex, and carboxymethyl Sephadex. A homogeneous preparation was obtained in over-all yield of about 50%. T...
متن کاملPurification and characterization of chicken pepsinogen and chicken pepsin.
Chicken pepsinogen was extracted from the forestomach of chicken and purified by the consecutive application of acetone precipitation, chromatography on diethylaminoethyl cellulose, and gel filtration on Sephadex G-100. The purified pepsinogen was homogeneous on disc electrophoresis and sedimented as monodisperse material. Chicken pepsin was obtained by the activation of the pure zymogen at pH ...
متن کاملDialyzable cofactor in nerve growth promoting protein from mouse salivary glands.
Cohen's method for preparing the nerve growth factor from mouse submaxillary glands was followed to the last ammonium sulfate fraction. Further purification was accomplished with carboxymethyl- and diethylaminoethyl- column chromatography. Three peaks were obtained for each column; the third peak obtained with diethylaminoethyl cellulose was the most active. Electrophoresis of this active fract...
متن کاملPurification and properties of pyridine nucleosidase (glycosidase) from bull semen.
A soluble pyridine nucleotidase was first described in bull semen by Leone and Bonaduce (1). During studies on the specificity of this enzyme, we observed that passage of dilute semen through a column composed of calcium phosphate gel and diethylaminoethyl cellulose anion exchanger (Whatman)] resulted in a preparation of high specific activity. In this single purification step the specific acti...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Biochemical journal
دوره 169 3 شماره
صفحات -
تاریخ انتشار 1978