Abstract
Carboxylic esterase activity toward the acetate and butyrate esters of α- and β-naphthol is associated with two forms of erythrocyte carbonic anhydrase (CA-I, CA-II) in man (Tashian et al. , 1963) and other primate species. Of 22 primate species tested, erythrocyte CA-I from the rhesus macaque ( Macaca mulatta ) and doguera baboon ( Papio doguera ) were among those forms showing high specific esterase activity; in comparison, human and chimpanzee ( Pan troglodytes ) CA-I exhibit moderate esterase activity. This report compares the hydrolase and hydrase activities of partially-purified CA-I from human, chimpanzee, baboon, and rhesus hemolysates.
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