Protein turnover during growth of the haloalkaliphilic archaeon Natronococcus occultus

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 📂 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