𝔖 Bobbio Scriptorium
✦   LIBER   ✦

One-step purification of cathepsin D by affinity chromatography using immobilized propeptide sequences

✍ Scribed by Sergio Wittlin; Johannes Rösel; David R. Stover

Book ID
114429021
Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
444 KB
Volume
252
Category
Article
ISSN
1432-1327

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Purification of pepsins and cathepsin D
Purification of pepsins and cathepsin D by affinity chromatography on Sepharose 4B with an immobilized synthetic inhibitor
✍ Jan Pohl; Milan Zaoral; Antonín Jindra Jr.; Vladimír Kostka 📂 Article 📅 1984 🏛 Elsevier Science 🌐 English ⚖ 759 KB

Val-D-Leu-Pro-Phe-Phe-Val-D-Leu, a specific inhibitor of aspartate proteinases of the pepsin type, was synthesized. Its bonding to activated 6-aminohexanoic acid-Sepharose 4B afforded an affinity support suitable for the purification of human, porcine, and chicken pepsin, human gastricsin, and bovin

One step purification procedure of elast
One step purification procedure of elastase from pancreatic powder by affinity chromatography
✍ Kenji Katagiri; Toshihiko Takeuchi; Keiko Taniguchi; Makoto Sasaki 📂 Article 📅 1978 🏛 Elsevier Science 🌐 English ⚖ 582 KB

Pancreatic elastase was isolated from acetone powder of porcine pancreas by a one step purification procedure on a trialanyl CH-Sepharose 4B affinity column. This column exhibited affinity not only for active elastase but also for trypsin and chymotrypsin which were present in the same pancreatic po