Topogenesis of carboxylesterases: a rat liver isoenzyme ending in -HTEHT-COOH is a secreted protein
| Autor: | Mariette Robbi, Henri Beaufay |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Time Factors
Immunoprecipitation Molecular Sequence Data Biophysics Biology Transfection Biochemistry Esterase symbols.namesake Carboxylesterase Complementary DNA Animals Amino Acid Sequence Cloning Molecular Molecular Biology Cells Cultured COS cells Genetic Variation Rats Inbred Strains Cell Biology Golgi apparatus Molecular biology Recombinant Proteins Rats Secretory protein symbols Microsomes Liver Mutagenesis Site-Directed Carboxylic Ester Hydrolases |
| Zdroj: | Biochemical and biophysical research communications. 183(2) |
| ISSN: | 0006-291X |
| Popis: | We have cloned a rat liver cDNA that encodes a carboxylesterase isoenzyme, as revealed by immunoprecipitation, cytochemical staining and inhibition by bis- p -nitrophenylphosphate of the product expressed in transfected COS cells. The predicted polypeptide ends in -HTEHT-COOH. The product is secreted by COS cells with a half-time of about 1 hour, after maturation of oligosaccharide chains in the Golgi complex. A variant ending in -HTEL-COOH is stable in the cells. This strengthens the existing evidence that the HXEL-COOH end signals proteins for retrieval from the secretory traffic in animal cells. The encoded enzyme still remains to be identified. It shows 98% homology to an esterase sequenced earlier (Takagi et al. 1988, J. Biochem. 104, 801–806; Long et al. 1988, Biochem. Biophys. Res. Commun. 156, 866–873); however it must be an enzyme from the serum, not from the microsomes. |
| Databáze: | OpenAIRE |
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