Nitration and Iodination of Human Carbonic Anhydrases

Human Carbonic Anhydrases

Sequence studies of human erythrocyte carbonic anhydrase B show that it contains 256 residues. A series of relatively small peptides soluble in aqueous solutions obtained by chymotryptic and tryptic digestion of the enzyme, large peptides containing only COOH-terminal lysine or arginine as well as those resulting from more limited cleavage of the enzyme, and cyanogen bromide cleavage products s...

Acid Difference Spectra of Human Carbonic Anhydrases.

Human carbonic anhydrase B loses enzymatic activity as it undergoes an irreversible conformational change near pH 4 (1). Riddiford (2) further found that seven of the eleven histidyl groups, which are unreactive in the native protein, become titratable during this change. Also, five or six of the eight tyrosyl groups do not ionize freely and reversibly in the native protein (2, 3). Human carbon...

Polyamines and α-Carbonic Anhydrases.

Natural products represent a straightforward source for molecular structures bearing a vast array of chemical features and potentially useful for biomedical purposes. Recent examples of this type include the discovery of the coumarins and the polyamine natural products as atypical chemotypes for the inhibition of the metalloenzymes carbonic anhydrases (CAs; EC 4.2.2.1). CA enzymes are establish...

Kinetic Studies of Human Carbonic Anhydrases B and C.

Purification and properties of human erythrocyte carbonic anhydrases.

Three different methods are described for separating hemoglobins from carbonic anhydrases in hemolysates from human erythrocytes. The preferred method involves adsorption on diethylaminoethyl Sephadex at pH 8.7 followed by selective elution of the carbonic anhydrases. Carbonic anhydrases A, B, and C are subsequently separated from each other on DEAE-Sephadex by elution with 0.05 M Trischloride ...