Rat kidney carboxylesterase. Cloning, sequencing, cellular localization, and relationship to rat liver hydrolase.

@article{Yan1994RatKC,
  title={Rat kidney carboxylesterase. Cloning, sequencing, cellular localization, and relationship to rat liver hydrolase.},
  author={Ben Yan and Dongfang Yang and Marcella Brady and Andrew Parkinson},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 47},
  pages={29688-96}
}
We recently purified from rat liver microsomes a carboxylesterase, designated hydrolase B, that catalyzes the hydrolysis of para-nitrophenylacetate with low affinity (Km approximately 400 microM) and is relatively insensitive to the inhibitory effects of phenylmethylsulfonyl fluoride. A carboxylesterase with identical properties is also present in rat kidney microsomes, at levels comparable to those in liver microsomes. The kidney enzyme is immunochemically indistinguishable from hydrolase B by… CONTINUE READING
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