Purification and biochemical characterization of alkaline serine protease from caesalpinia bonducella
A high molecular weight serine protease has been purified to electrophoretic homogeneity from the seeds of Caesalpinia bonducella Hem. (Caesalpiniaceae) by the combination of size exclusion and ion exchange chromatography. About 524 fold purification was achieved with an overall recovery of 6.8%. Th...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Published: |
Natural Products Inc
2010
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