Immunoaffinity purification of human prorenin produced in Chinese hamster ovary cells.
A simple immunoaffinity column chromatographic procedure is described whereby recombinant human prorenin secreted from Chinese hamster ovary cells may be isolated in a high state of purity from serum-free culture medium. Prorenin thus purified has been characterized by SDS-polyacrylamide gel electrophoresis and by partial sequence analysis which has revealed the expected N-terminal sequence. Trypsin treatment gives rise to renin, and reversible acid activation has also been demonstrated for the recombinant zymogen.
Ishizuka
Y
Y
Institute of Applied Biochemistry, University of Tsukuba, Japan.
Saito
M
M
Hori
H
H
Poorman
R A
RA
Yoshida
S
S
Murakami
K
K
D000645:Ammonium Sulfate; D000818:Animals; D002460:Cell Line; D011232:Chemical Precipitation; D002846:Chromatography, Affinity; D006224:Cricetinae; D003412:Cricetulus; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism; D005260:Female; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007118:Immunoassay; D008970:Molecular Weight; D010053:Ovary / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism; D012083:Renin / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism; D014357:Trypsin
D004792:Enzyme Precursors; D011994:Recombinant Proteins; D014357:Trypsin; D012083:Renin; D000645:Ammonium Sulfate