Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other carboxylesterases, and their possible function.

@article{Mentlein1985SpecificityOT,
  title={Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other carboxylesterases, and their possible function.},
  author={Rolf Mentlein and Gerd Reuter and Eckhard W. Heymann},
  journal={Archives of biochemistry and biophysics},
  year={1985},
  volume={240 2},
  pages={
          801-10
        }
}
One of the previously described five purified monoglyceride-cleaving carboxylesterases from rat liver microsomes proved to be a carnitine ester hydrolase. This esterase, with an isoelectric point of 5.2, is most active with medium-chain acyl-L-carnitines (C12-C14). The esterase is also remarkably active with 1,3-diglycerides, especially 1,3-dioctanoylglycerol, that are hydrolyzed faster than the corresponding 1-monoglycerides and triglycerides. Only one of the other four purified… CONTINUE READING