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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Carboxylic Ester Hydrolases / biosynthesis*
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Carboxylic Ester Hydrolases / genetics
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Carboxylic Ester Hydrolases / metabolism
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Cell Line
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Cloning, Molecular
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Kinetics
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Liver / enzymology*
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Membrane Glycoproteins / biosynthesis*
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / metabolism
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Mice
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Molecular Sequence Data
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Rats
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Substrate Specificity
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Transfection
Substances
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Membrane Glycoproteins
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Recombinant Proteins
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Carboxylic Ester Hydrolases
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egasyn