Abstract
Renin binding protein (RnBP) is a proteinous renin inhibitor. This protein binds to renin forming a protein complex, so-called high molecular weight (HMW) renin. The protein complex has been confirmed by purification and characterization of HMW renin [1] and RnBP from porcine kidney [2, 3]. Recently, cDNA clones encoding RnBPs were isolated from porcine, human and rat kidney cDNA libraries [4, 5]. The amino acid sequences, which were deduced from the nucleotide sequences, were highly homologous and characterized by the presence of a conserved leucine-zipper motif. This motif plays an essential role in the formation of an RnBP homodimer and an RnBP-renin heterodimer [6]. The present study describes the biochemical and molecular biological properties of RnBPs.
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