Inhibition and Chemical Modifications of Human Erythrocyte Carbonic Anhydrase B

Specific chemical modification studies were carried out in an attempt to characterize the "active site" of carbonic anhydrase with regard to its catalytic properties, the binding of inhibitors (anions and sulfonamides), and the binding and role of the zinc atom. Enzymatic activity was dete...

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Veröffentlicht in:	The Journal of biological chemistry 1967-09, Vol.242 (18), p.4212-4220
Hauptverfasser:	Whitney, P L, Nyman, P O, Malmström, B G
Format:	Artikel
Sprache:	eng
Schlagworte:	Amides Amidines Binding Sites Carbonic Anhydrase Inhibitors Carbonic Anhydrases - analysis Chlorides Coenzymes Erythrocytes - enzymology Histidine Humans Hydrogen-Ion Concentration Lysine Sulfanilamides Zinc
Online-Zugang:	Volltext
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