Abstract
The human neurokinin-1 receptor has been expressed in insect cells using a recombinant baculovirus. The expression level is about 10 times higher than that obtained in mammalian cells. The recombinant receptor was solubilized with CHAPS, and a PEG precipitation procedure was shown to be effective in regaining high affinity substance P binding. This system should allow large scale purification of the human neurokinin-1 receptor.
MeSH terms
-
Animals
-
Base Sequence
-
Cholic Acids
-
Cloning, Molecular
-
Detergents
-
Genetic Vectors*
-
Humans
-
Insecta / cytology
-
Insecta / metabolism*
-
Molecular Sequence Data
-
Nucleopolyhedroviruses / genetics*
-
Receptors, Neurokinin-1 / biosynthesis
-
Receptors, Neurokinin-1 / genetics*
-
Recombinant Proteins / biosynthesis
-
Solubility
Substances
-
Cholic Acids
-
Detergents
-
Receptors, Neurokinin-1
-
Recombinant Proteins
-
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate