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Expression of enzymatically active enkephalinase (neutral endopeptidase) in mammalian cells
Author(s) -
Gorman Cornelia M.,
Gies David,
Schofield Peter R.,
KadoFong Helen,
Malfroy Bernard
Publication year - 1989
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240390307
Subject(s) - enkephalinase , complementary dna , neprilysin , microbiology and biotechnology , thiorphan , transfection , plasmid , endopeptidase , biology , enzyme , chemistry , biochemistry , gene , receptor , opioid , enkephalin
A cDNA encoding the rat enkephalinase protein (neutral endopeptidase; EC 3.4.24.11) has been constructed from overlapping > 10 cDNA clones. This cDNA was inserted into an expression plasmid containing the cytomegalovirus enhancer and promoter. When transfected with this plasmid, Cos 7 cells transiently expressed the enkephalinase protein in a membrane‐bound state. Recombinant enkephalinase recovered in solubilized extracts from transfected Cos 7 cells was enzymatically active and displayed properties similar to those of the native enzyme with respect to sensitivity to classical enkephalinase inhibitors.