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The primary structure of the human placental ribonuclease inhibitor (PRI), a tight-binding inhibitor of angiogenin and pancreatic ribonucleases, has been determined from the cDNA. The sequence of the mature protein is composed of 460 amino acids, yielding a molecular mass of 49,847 g/mol. Peptides comprising 92% of the predicted sequence were isolated from a tryptic digest of PRI, and direct sequence information obtained for 65% of the molecule agreed at all positions with the sequence predicted from the cDNA. The amino acid sequence of PRI contains seven direct internal repeat units, each 57 amino acids in length. These repeat units comprise 87% of the molecule. The average degree of identity between any two is 39%. A region within each repeat unit displays similarity to tandem, leucine-rich repeats found in six other proteins. Modification of PRI with iodoacetic acid, p-(hydroxymercuri)benzoate, and 5,5'-dithiobis(2-nitrobenzoic acid) reveals that at least 30 of the 32 cysteine residues of PRI are in the reduced form.
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