Immunoaffinity purification of human prorenin produced in Chinese hamster ovary cells |
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| Authors: | Y Ishizuka M Saito H Hori R A Poorman S Yoshida K Murakami |
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| Affiliation: | Institute of Applied Biochemistry, University of Tsukuba, Japan. |
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| Abstract: | 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. |
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