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Active prorenin: Evidence for the formation of a conformational variant of recombinant human prorenin

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Abstract

Using highly purified recombinant human prorenin, we report the first evidence for the formation of a stable, partially active, conformational variant of the recombinant proenzyme. The enzymatically active prorenin exhibits the following characteristics: (1) the proenzyme N-terminal sequence and molecular weight are maintained; (2) the active proenzyme is capable of cleaving a novel fluorogenic peptide substrate based on the sequence of human angiotensinogen and exhibits about 30% of mature renin specific activity for the fluorogenic substrate; (3) the active proenzyme conformation binds to, and can be eluted from, a pepstatin affinity column; and (4) the activity of the active proenzyme can be inhibited by a novel peptidomimetic renin inhibitor.

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Edalji, R., Holzman, T.F. & Gubbins, E.J. Active prorenin: Evidence for the formation of a conformational variant of recombinant human prorenin. J Protein Chem 10, 403–406 (1991). https://doi.org/10.1007/BF01025254

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  • DOI: https://doi.org/10.1007/BF01025254

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