Large-scale preparation and biological activity of recombinant human parathyroid hormone.
Human parathyroid hormone (hPTH) has been bacterially expressed in bioreactors as cro-beta-galactosidase-hPTH fusion protein. We have developed a large-scale purification scheme that exploits the pH-dependent differential solubility of hPTH and a two-step chromatographic procedure. We demonstrate that in a number of assay systems, the recombinant material obtained by this procedure is biologically active.
Paulsen
J
J
Gesellschaft für Biotechnologische Forschung mbH, Braunschweig, Germany.
Ochs
D
D
Harder
M
M
Duvos
C
C
Mayer
H
H
Wingender
E
E
D000818:Animals; D001842:Bone and Bones / Q000378:metabolism; D002118:Calcium / Q000378:metabolism; D002455:Cell Division / Q000187:drug effects; D002478:Cells, Cultured; D002642:Chick Embryo; D002851:Chromatography, High Pressure Liquid; D000242:Cyclic AMP / Q000096:biosynthesis; D005285:Fermentation; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D009924:Organ Culture Techniques; D010281:Parathyroid Hormone / Q000235:genetics* / Q000378:metabolism / Q000494:pharmacology; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D001616:beta-Galactosidase / Q000235:genetics / Q000378:metabolism
D010281:Parathyroid Hormone; D011993:Recombinant Fusion Proteins; D000242:Cyclic AMP; D001616:beta-Galactosidase; D002118:Calcium