Semi-preparative purification of recombinant human renin and prorenin.
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.
Carilli
C T
CT
California Biotechnology, Inc., Mountain View 94043.
Wallace
L C
LC
Smith
L M
LM
Wong
M A
MA
Lewicki
J A
JA
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*
D004792:Enzyme Precursors; D011994:Recombinant Proteins; D012083:Renin