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Title: Purification of mouse Ren 2 prorenin produced in Chinese hamster ovary cells. Author: Hatsuzawa K, Kim WS, Murakami K, Nakayama K. Journal: J Biochem; 1990 Jun; 107(6):854-7. PubMed ID: 2202716. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]