Fractionation and purification of the thiol proteinases from papaya latex
| Autor: | Joseph Demeester, Philippe Dekeyser, Albert Lauwers, Stefaan C. De Smedt |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Chromatography
Latex biology Hydrophilic interaction chromatography Native Polyacrylamide Gel Electrophoresis Chymopapain General Chemistry Hydrogen-Ion Concentration Plants Chromatography Ion Exchange Glycyl endopeptidase Amidohydrolases Active center Cysteine Endopeptidases chemistry.chemical_compound Papain chemistry biology.protein Electrophoresis Polyacrylamide Gel Protease Inhibitors Sodium dodecyl sulfate Plant Proteins Caricain |
| Zdroj: | Journal of Chromatography B: Biomedical Sciences and Applications. 656:203-208 |
| ISSN: | 0378-4347 |
| DOI: | 10.1016/0378-4347(94)00083-2 |
| Popis: | Three cysteine proteinases, i.e. chymopapain, papaya proteinase IV and proteinase III, were purified to homogeneity from papaya latex using a combination of ion-exchange chromatography and hydrophobic interaction chromatography. During the purification procedure, the thiol-groups of the active center were reversibly blocked as mixed disulfides with 2-thiopyridone. Homogeneity was proved electrophoretically by native polyacrylamide gel electrophoresis (PAGE), sodium dodecyl sulfate (SDS)-PAGE and rechromatography on a Mono S 5/5 column at pH 5.0. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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