Nucleotide and deduced amino acid sequence of bovine adrenal medulla chromogranin B (secretogranin I)

David K. Grandy, Richard Leduc, Haripriya Makam, Thomas Flanagan, Emanuel J. Diliberto, Olivier Civelli, O. Humberto Viveros

    Research output: Contribution to journalArticlepeer-review

    4 Scopus citations


    1. A novel 1745-dalton pyroglutamyl peptide (BAM-1745) was recently isolated and characterized from bovine adrenal medulla chromaffin granules. Its amino acid sequence was found to be 93% identical to residues 580-593 of human chromogranin B (secretogranin I). 2. Based on this sequence a degenerate oligonucleotide probe was synthesized and used to identify a 2.4-kb bovine adrenal medulla chromogranin B cDNA. 3. The deduced polypeptide is 647 amino acids long and begins with a putative signal sequence of 20 residues as in the human, rat, and mouse proteins. Also conserved in the bovine protein is a tyrosine residue which may be sulfated, two N-terminal cysteines, and many paired basic amino acids which may serve as sites of posttranslational processing. The peptide BAM-1745 is flanked by paired basic amino acids and therefore is most likely a product of posttranslational processing. Bovine chromogranin B is 67, 58, and 58% identical to the human, rat, and mouse chromogranin B proteins, respectively. 4. The carboxyl terminus of bovine chromogranin B, including BAM-1745, was found to be the most conserved region of the polypeptide and may identify it as an important functional domain.

    Original languageEnglish (US)
    Pages (from-to)185-192
    Number of pages8
    JournalCellular and Molecular Neurobiology
    Issue number2
    StatePublished - Apr 1992


    • chromogranin B
    • nucleotide sequence
    • pyroglutamyl peptide
    • secretogranin I
    • sequence comparison

    ASJC Scopus subject areas

    • Cellular and Molecular Neuroscience
    • Cell Biology


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