Production of human renin in microorganism and its application to medicine.

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1) The primary structure of human renin precursor was deduced from its complementary sequence. The predicted sequence consists of 406 amino acids with a pre- and a prosegment carrying 20 and 46 amino acids, respectively.2) A three-dimensional model of human renin has been constructed based on the assumption that the overall folding of the aspartyl proteases is very similar. As a reference, we used penicillopepsin.3) The human renin gene was isolated from a Charon 4A human genomic library and characterized. The gene spans about 11.7 kilobases and consists of 10 exons and 9 introns that map at points that could be variable surface loops of the enzyme.4) Human prorenin was produded under the transcriptional control of the E. coli trp promoter-operator in the expression vector. The transformed E. coli cell expressed high levels (30% of total cell protein) of prorenin as part of a hybrid protein.