Specificity of esterases and structure of prodrug esters: reactivity of various acylated acetaminophen compounds and acetylaminobenzoated compounds.

@article{Seki1988SpecificityOE,
  title={Specificity of esterases and structure of prodrug esters: reactivity of various acylated acetaminophen compounds and acetylaminobenzoated compounds.},
  author={Hideichi Seki and Takanori Kawaguchi and Tsunehiko Higuchi},
  journal={Journal of pharmaceutical sciences},
  year={1988},
  volume={77 10},
  pages={855-60}
}
The relative rates of enzymatically catalyzed hydrolysis of various esters of p-acetylaminobenzoic acid (APAB) and variously acylated acetaminophen (APAP) derivatives were measured. Neutral, anionic, and cationic esters were examined. The enzyme sources adopted were rat intestinal homogenate, rat liver homogenate, rat plasma, and a partly purified commercial enzyme. In both APAB and APAP esters, neutral esters were the most sensitive of the enzyme sources examined, and the sensitivity was due… CONTINUE READING

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