Aspirin Esterase Research Articles

Aspirin Esterase of Gastric Mucosal Origin

The enzyme, aspirin esterase, which converts acetylsalicyclic acid to the less toxic salicyclic acid, was found to be present in gastric mucosal specimens obtained from surgically resected tissue. The enzyme was found to be stable to storage and active at two pH optima. Alcohol in the reaction mixture produced a net effect of slowing the rate of aspirin hydrolysis; this was attributable to a marked inhibitory effect on aspirin esterase activity which was not completely counteracted by the increased rate of spontaneous breakdown of aspirin by alcohol. Age, sex, or gastric disease state of the patient from whom the tissue was obtained, did not significantly alter the level of enzyme activity measured, nor were different levels obtained from body or antral mucosa. In patients with gastric ulcer, those with a previous history of regular aspirin consumption did not show significantly different levels from those without such a history. It is concluded that aspirin esterase activity of gastric mucosa is not alone a significant factor in any role acetylsalicyclic acid may play in the etiology and natural history of chronic peptic ulcer.

Correlation of serum aspirin esterase activity and half-life of salicylic acid.

An inverse correlation was found between the serum aspirin esterase activity in human subjects and the biological half-life of salicylic acid in serum and a direct relationship between the values of the elimination rate constant and the activity of this enzyme. The rate of acetylsalicylic acid breakdown may be one of the factors which influences the biological half-life of salicylates in the organism and may participate also in determining the individual response to the administered drug.

Studies on the aspirin esterase and paranitrophe-nylacetate esterase activities in the congestive heart failure

Studies on the aspirin esterase and paranitrophe-nylacetate esterase activities in the congestive heart failure