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    Biochem Biophys Res Commun. 1988 Feb 15;150(3):1275-81.

    Cloning of cDNA encoding a new peptide C-terminal alpha-amidating enzyme having a putative membrane-spanning domain from Xenopus laevis skin.

    Ohsuye K, Kitano K, Wada Y, Fuchimura K, Tanaka S, Mizuno K, Matsuo H.

    Suntory Institute for Biomedical Research, Osaka, Japan.

    A cDNA clone encoding a precursor of a peptide C-terminal alpha-amidating enzyme (AE-I) from Xenopus laevis skin was recently isolated and sequenced in our laboratory. In this study, by using the restriction fragment of this clone as a hybridization probe, we have identified the cDNA encoding another new peptide C-terminal alpha-amidating enzyme (tentatively named AE-II) distinct from AE-I. The cDNA encodes a polypeptide of 875 amino acid residues, which contains a region extensively homologous to AE-I precursor at N-terminus. The encoded protein characteristically has a putative membrane-spanning domain near C-terminus. Our results indicate that C-terminal alpha-amide formation of peptides in Xenopus skin is regulated by at least two distinct alpha-amidating enzymes.

    PMID: 2829895 [PubMed - indexed for MEDLINE]

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