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Purification and characterization of a membrane-associated ATPase from Natronococcus occultus, a haloalkaliphilic archaeon

✍ Scribed by Melinda L Eddy; Peter E Jablonski

Book ID
117516477
Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
178 KB
Volume
189
Category
Article
ISSN
0378-1097

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Purification and biochemical characteriz
Purification and biochemical characterization of the haloalkaliphilic archaeon Natronococcus occultus extracellular serine protease
✍ Claudia Alicia Studdert; Maria Karina Herrera Seitz; Maria Ines Plasencia Gil; J πŸ“‚ Article πŸ“… 2001 πŸ› John Wiley and Sons 🌐 English βš– 93 KB πŸ‘ 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