Purification and Biochemical Characterization of Alkaline Serine Protease from
A high molecular weight serine protease has been purified to electrophoretic homogeneity from the seeds of Caesalpinia bonducella Flem. (Caesalpiniaceae) by the combination of size exclusion and ion exchange chromatography. About 524 fold purification was achieved with an overall recovery of 6.8%. T...
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| Principais autores: | , , , , , , , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
SAGE Publishing
2010-06-01
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| Serier: | Natural Product Communications |
| Online adgang: | https://doi.org/10.1177/1934578X1000500625 |
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