Purification of mouse Ren 2 prorenin produced in Chinese hamster ovary cells.
Renin is produced from a larger, inactive precursor, prorenin, by endoproteolytic removal of the amino-terminal prosegment. In this study, we have transfected Chinese hamster ovary cells with the expression plasmid of mouse Ren 2 preprorenin, and have purified mouse Ren 2 prorenin from the incubation medium of these cells by DEAE-Toyopearl chromatography, Blue-Toyopearl chromatography, and isoelectric focusing. Prorenin thus purified has a molecular mass of 42 kDa as determined by SDS-PAGE and an isoelectric point of 6.5. Amino-terminal sequencing has demonstrated that the purified prorenin has the amino-terminus predicted from the nucleotide sequence of mouse Ren 2 preprorenin cDNA.
Hatsuzawa
K
K
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki.
Kim
W S
WS
Murakami
K
K
Nakayama
K
K
D000818:Animals; D002478:Cells, Cultured; D006224:Cricetinae; D004792:Enzyme Precursors / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification*; D051379:Mice; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification; D012083:Renin / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification*; D013363:Submandibular Gland / Q000201:enzymology*; D014162:Transfection
D004792:Enzyme Precursors; D011994:Recombinant Proteins; D012083:Renin