Purification and characterization of human pancreatic phospholipase A2
| Autor: | Jarkko Uolevi Eskola, H J Aho, Timo J. Nevalainen |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
chemistry.chemical_classification
Chemistry Isoelectric focusing Biochemistry (medical) Clinical Biochemistry Phospholipase Zymogen granule Molecular biology chemistry.chemical_compound medicine.anatomical_structure Isoelectric point Enzyme Biochemistry medicine Sodium dodecyl sulfate Pancreas Polyacrylamide gel electrophoresis |
| Zdroj: | Clinical Chemistry. 29:1772-1776 |
| ISSN: | 1530-8561 0009-9147 |
| DOI: | 10.1093/clinchem/29.10.1772 |
| Popis: | We purified human pancreatic phospholipase A2 from postmortem pancreatic tissue by elution of the semi-purified enzyme on CM-Sephadex C-25 with a linear NaCl gradient at pH 6.0. The enzyme appeared as a single polypeptide chain with an isoelectric point of 9.2 +/- 0.1. The relative molecular mass of the enzyme was estimated to be 15 800 +/- 1000 by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. The enzyme is resistant to heating and to a 25 g/L concentration of sodium dodecyl sulfate. It is inhibited by Ca2+ ions in the presence of ovolecithin and deoxycholate. By immunohistochemical methods we showed the enzyme to be localized in the apical zymogen granule portion of pancreatic acinar cells. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|