title: Semi-preparative purification of recombinant human renin and prorenin.
abstract: Chinese hamster ovary (CHO) cells, transfected with a vector containing cDNA coding for preprorenin, have been shown to secrete authentic prorenin into the culture supernatant. Purification of the expressed prorenin and purification of active renin, generated by solid-phase trypsin treatment of the conditioned media, have been achieved by conventional chromatographic methods. Scale-up of the initial steps of these procedures is described, including the use of radial-flow columns and automation with fast protein liquid chromatography valves and pumps. This semi-preparative scheme has allowed hundreds of milligrams of both proteins to be isolated.
authors.affiliation: California Biotechnology, Inc., Mountain View 94043.
authors.forename: C T
authors.initials: CT
authors.lastname: Carilli
authors.forename: L C
authors.initials: LC
authors.lastname: Wallace
authors.forename: L M
authors.initials: LM
authors.lastname: Smith
authors.forename: M A
authors.initials: MA
authors.lastname: Wong
authors.forename: J A
authors.initials: JA
authors.lastname: Lewicki
mesh_terms: D002460:Cell Line; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004792:Enzyme Precursors / Q000302:isolation & purification*; D006801:Humans; D011994:Recombinant Proteins / Q000302:isolation & purification; D012083:Renin / Q000302:isolation & purification*
chemical_list: D004792:Enzyme Precursors; D011994:Recombinant Proteins; D012083:Renin