Purification and characterization of two rat liver microsomal carboxylesterases (hydrolase A and B).

@article{Morgan1994PurificationAC,
  title={Purification and characterization of two rat liver microsomal carboxylesterases (hydrolase A and B).},
  author={E W Morgan and Ben Yan and D J Greenway and Dennis R. Petersen and Andrew Parkinson},
  journal={Archives of biochemistry and biophysics},
  year={1994},
  volume={315 2},
  pages={495-512}
}
The enzymatic hydrolysis of para-nitrophenylacetate by rat liver microsomes is predominantly catalyzed by two esterases: one with high affinity (Km approximately 25 microM) and one with low affinity (Km approximately 400 microM) for the substrate. Two kinetically distinct esterases were similarly detected in liver microsomes from mouse, hamster, guinea pig, rabbit, cat, cynomolgus monkey, and human, but only the high-affinity enzyme was detectable in dog liver microsomes. The tissue… CONTINUE READING

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