Abstract
The biochemical properties of an INH acetylating enzyme protein of liver homogenates from rhesus monkeys were studied. The enzyme was purified about 250-fold. Studies of substrate specificity to aliphatic and aromatic compounds as well as comparison of the structure of some competitive inhibitors were performed. Serotonin is acetylated to acetyl serotonin with high affinity to the INH acetylating enzyme. Enzyme preparations from so-called rapid and slow acetylating animals show different specific activities, but similar properties regarding purification values, K m 0-values of INH, inhibitor constants of some aromatic compounds. Comparing arylamine acetylase of pigeon liver with the acetylating system of rhesus-liver, we stated characteristic differences.
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