Cloning and Sequencing of Rat-liver Carboxylesterase Es-3 (egasyn)
(1994) Biochemical and Biophysical Research Communications — Vol. 203, n° 3, p. 1404-1411 (1994)
Files
pdfdocument.pdf
Restricted Access - Adobe PDF
- 380.68 KB
Details
- Authors
- Abstract
- The cDNA of the rat carboxylesterase ES-3 encodes a polypeptide with 561 amino acid residues including a cleavable signal peptide at the N-terminus. The processed polypeptide shows over 90 % sequence identity to mouse egasyn (ES-22); its calculated pI (5.5) matches the value determined for purified liver ES-3. The product expressed in COS cells migrates in native gels in the region of ES-3 and is similarly active on acetanilide. It is retained in the cells, as predicted from its C-terminus HTEL, and bears a single endo-H sensitive oligosaccharide chain. The nonglycosylated form expressed in the presence of tunicamycin is also intracellular, but substantially less active. (C) 1994 Academic Press, Inc.
- Affiliations
Citations
Robbi, M., & Beaufay, H. (1994). Cloning and Sequencing of Rat-liver Carboxylesterase Es-3 (egasyn). Biochemical and Biophysical Research Communications, 203(3), 1404-1411. https://doi.org/10.1006/bbrc.1994.2341 (Original work published 1994)