Ultramicroanalysis of pH,(P_{CO_2 } )and carbonic anhydrase activity at calcifying sites in cartilage

Crystallographic studies of inhibitor bi

Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: A pentacoordinated binding of the SCN− ion to the zinc at high pH

✍ A. Elisabeth Eriksson; Per M. Kylsten; T. Alwyn Jones; Anders Liljas 📂 Article 📅 1988 🏛 John Wiley and Sons 🌐 English ⚖ 961 KB

The binding of four inhibitors--mercuric ion, 3-acetoxymercuri-4-aminobenzenesulfonamide (AMS), acetazolamide (Diamox), and thiocyanate ion--to human carbonic anhydrase II (HCA II) has been studied with X-ray crystallography. The binding of mercury to HCA II at pH 7.0 has been investigated at 3.1 A