The primary structure of the human renin precursor, consisting of 406 amino acids with pre and pro segments, was deduced from its cloned cDNA sequence.
The study deduced the primary structure of the human renin precursor, revealing its 406 amino acid sequence and structural similarities to aspartyl proteinases.
The primary structure of human renin precursor has been deduced from its cDNA sequence. A library of cDNA clones was constructed from human kidney poly(A)+ RNA by applying the vector/primer method of Okayama and Berg. The library was screened for human renin sequences by hybridization with the previously cloned mouse renin cDNA. Of the 240,000 colonies screened, 35 colonies that were positive for hybridization were isolated. Two recombinant plasmids containing long inserts of about 1,300 and 1,600 base pairs were selected for sequence analysis. The amino acid sequence predicted from the cDNA sequence shows that the human renin precursor consists of 406 amino acids with a pre and a pro segment carrying 20 and 46 amino acids, respectively. A high degree of sequence homology was found upon comparison of the mouse and human renins. Close similarities were also observed in the primary structures of renin and aspartyl proteinases that have known three-dimensional structures, suggesting a similar tertiary structure for renin.
Imai et al. (1983) studied Severe renovascular hypertension. The primary structure of the human renin precursor, consisting of 406 amino acids with pre and pro segments, was deduced from its cloned cDNA sequence.
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