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J. Biochem, 1990, Vol. 107, No. 6 854-857
© 1990 Japanese Biochemical Society

research-article

Purification of Mouse Ren 2 Prorenin Produced in Chinese Hamster Ovary Cells1

Kiyotaka Hatsuzawa*, Won-Sin Kim*, Kazuo Murakami*,** and Kazuhisa Nakayama**,***,2

*Institute of Applied Biochemistry
**Gene Experiment Center
***Institute of Biological Sciences, University of Tsukuba Tsukuba 305

2 To whom correspondence should be addressed.

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.

1This study was supported in part by grants from the Ministry of Education, Science and Culture of Japan, from University of Tsukuba Project Research, and from Chichibu Cement Co.


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