STUDIES ON THE ESTERASE OF TUBERCLE BACILLI AND VARIOUS STRAINS OF ACID-FAST BACILLI (II)

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ESTERASE activities of various acid-fast bacilli and their extracts were measured by Rona and Lasnitzki's method. 1. The esterase activity of avian tubercle bacilli was heat-stable irrespective of cultural conditions. 2. There were two different types of esterases in acid-fast bacilli, heat-stable esterase (Esterase II) of avian type and heat-labile esterase (Esterase I) of thymotee type. 3. Esterase II was further subdivided into two different esterases, one being the butyl ester hydrolyzing esterase and the other being acetyl ester hydrolyzing esterase. The former was the most heat-stable (stable against the heating at 100°C for 30 minutes) and was inhibited markedly by oleio acid, iodine and atoxyl. The latter was inactivated by heating at 100°C for 20 minutes (stable against the heating at 80°C for 10 minutes) and fairly resistant against the influence of inhibitors. Subdivision of Esterase I (heat-labile) was not practicable. 4. Purification by adsorption on silicious earth, fractionation with ammonium sulfate and acetone increased the butyl ester hydrolyzing activity of Esterase II about 15 times. The purified esterase was also heat-stable and had the characteristics of protein or polypeptide. By paper chromatography, 13 amino acids were shown in the acid hydrolysate of the purified esterase. The esterase activity was inhibited markedly by iodine, oleic acid and eserine.
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