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Extracellular protease ofNatrialba magadii: purification and biochemical characterization

✍ Scribed by María I. Giménez; Claudia A. Studdert; Jorge J. Sánchez; R. E. De Castro


Publisher
Springer
Year
2000
Tongue
English
Weight
139 KB
Volume
4
Category
Article
ISSN
1431-0651

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Purification and biochemical characteriz
✍ Claudia Alicia Studdert; Maria Karina Herrera Seitz; Maria Ines Plasencia Gil; J 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 93 KB 👁 1 views

A serine protease was purified from Natronococcus occultus stationary phase culture medium (328-fold, yield 19%) and characterized at the biochemical level. The enzyme has a native molecular mass of 130 kDa, has chymotrypsin-like activity, is stable and active in a broad pH range (5.5 -12), is rathe