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Abstract
The activity of partially purified erythrocyte acid phosphatase (EAPase) was enhanced by alcohols, 7.6-fold by methanol, 4-fold by butanol, 3-fold by propanol, and 2.6-fold by ethanol and by pentanol. The carbon number of the aliphatic alcohols was proportional to the activation rate (defined as half the most activated value per the alcohol concentration) of EAPase, except in the case of ethanol. This rule was also applicable to human prostatic acid phosphatase (PAPase). However, the extent of PAPase activation by alcohols was lower than that of EAPase. In the presence of polyhydric alcohols, sorbitol, glycerin, and ethylene glycol, the extent of activation of EAPase was found to be proportional to the number of hydroxyl groups of the alcohols. The activation of EAPase was analyzed by means of the Lineweaver-Burk plot, and was found to be noncompetitive. PAPase activation by aliphatic alcohols was also noncompetitive.
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