Active prorenin: Evidence for the formation of a conformational variant of recombinant human prorenin |
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Authors: | Rohinton Edalji Thomas F Holzman and Earl J Gubbins |
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Institution: | (1) Protein Biochemistry, Pharmaceutical Discovery Research, Pharmaceutical Products Division, Abbott Laboratories, 60064 Abbott Park, Illinois;(2) Molecular Biology, Pharmaceutical Discovery Research, Pharmaceutical Products Division, Abbott Laboratories, 60064 Abbott Park, Illinois |
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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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Keywords: | Prorenin renin protein folding N-terminal sequence conformation |
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