Rat pancreatic and salivary amylase [( 1 -4) a-D-gkan glucanohydrolase] (EC 3.2.1.1) were purified 20-to 50-fold with a yield above 75% by a single-step affinity chromatographic procedure. The affinity ligand was an a-glucohydrolase inhibitor (proprietary name Bay g5421) coupled to w-aminohexyl-Seph
One step purification procedure of elastase from pancreatic powder by affinity chromatography
✍ Scribed by Kenji Katagiri; Toshihiko Takeuchi; Keiko Taniguchi; Makoto Sasaki
- Publisher
- Elsevier Science
- Year
- 1978
- Tongue
- English
- Weight
- 582 KB
- Volume
- 86
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
✦ Synopsis
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 powder. However, as the extent of affinity toward elastase is considerably higher, the proper conditions were determined with which the adsorbed elastase was isolated in a highly purified form. The yield of elastolytic activity ranged from 60-85% and the purified elastase was shown to be one component by polyacrylamide disc electrophoresis.
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