Cloning, functional expression, and characterization of recombinant pig liver esterase.

@article{Lange2001CloningFE,
  title={Cloning, functional expression, and characterization of recombinant pig liver esterase.},
  author={Stefan F Lange and Anna Musidlowska and Claudia Schmidt-Dannert and Jutta Schmitt and Uwe T Bornscheuer},
  journal={Chembiochem : a European journal of chemical biology},
  year={2001},
  volume={2 7-8},
  pages={576-82}
}
The N-terminal amino acid sequence of pig liver esterase (PLE) from a commercial sample was determined and shown to match closely to a published sequence encoding a proline-beta-naphthylamidase from pig liver. Next, mRNA isolated from pig liver was transcribed into cDNA and primers deduced from the N-terminal sequence were used to clone the 1698 base pairs of PLE cDNA. Initial attempts to express the cDNA in Escherichia coli and Pichia pastoris with different expression vectors and secretion… CONTINUE READING
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