Abstract：
:Porcine LH receptor ectodomain was overexpressed in insect cells and lepidopteran larvae using the recombinant baculovirus expression system. A low multiplicity of infection yielded the largest active production, of approximately 10(7) receptors/cell or 3 micrograms active receptor/mg total protein in infected cells. The truncated ectodomain solubilized with Triton X-100 bound its ligand with a high affinity which was comparable with that of the native membrane receptor. Increasing the multiplicity of infection resulted in an optimum protein production of 0.6 mg receptor/mg total protein in infected cells. This receptor was largely inactive, probably trapped within aggregation pools. Active receptor could be recovered by dilution of the samples. No secretion of recombinant receptor was ever observed whatever the conditions of infection. Expression of the recombinant receptor in insect larvae was also tested. This low-cost system failed both to increase the amount of active receptor and to induce secretion into the haemolymph. Two methods remain for producing sizeable amounts of active receptor with this baculovirus/insect cell system. One relies on immunoaffinity purification of the active protein and requires large-scale production, and the other is based on the purification of overexpressed inactive receptor followed by renaturation.
journal_name
J Mol Endocrinoljournal_title
Journal of molecular endocrinologyauthors
Pajot-Augy E,Couture L,Bozon V,Remy JJ,Biache G,Severini M,Huet JC,Pernollet JC,Salesse Rdoi
10.1677/jme.0.0140051subject
Has Abstractpub_date
1995-02-01 00:00:00pages
51-66issue
1eissn
0952-5041issn
1479-6813journal_volume
14pub_type
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