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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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Бібліографічні деталі
Автори: Hidayatullah Khan, Irshad Ali, Arif-ullah Khan, Mushtaq Ahmed, Zamarud Shah, Ahmad Saeed, Rubina Naz, Mohamad Rais Mustafa, Atiya Abbasi
Формат: Artigo
Мова:Inglês
Опубліковано: SAGE Publishing 2010-06-01
Серія:Natural Product Communications
Онлайн доступ:https://doi.org/10.1177/1934578X1000500625
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