Relationship of multiple forms of chromogranin

J. Settleman, R. Fonseca, J. Nolan, R. H. Angeletti

Research output: Contribution to journalArticle

56 Scopus citations


Chromogranin polypeptides of M(r) 100,000, M(r) 85,000, M(r) 75,000, and M(r) 65,000 have been detected in adrenal medulla chromaffin granules using anti-chromogranin antiserum. Monoclonal antibodies to this protein also detect the multiple molecular weight chromogranin polypeptides. Analysis of phosphorylated amino acids gives a value of 5 phosphoserine residues/mol of M(r) 75,000 chromogranin polypeptide. Immunological analysis of dephosphorylated chromogranin shows that the anti-chromogranin serum reacts with both the phosphorylated and unphosphorylated forms of the protein. Each of the chromogranin polypeptides has been isolated using a combination of DEAE-cellulose chromatography and reverse phase high pressure liquid chromatography. Sequencer analysis of each protein revealed a high degree of amino acid identities at the amino terminal of these proteins. Amino-terminal Sequencer analysis of chromogranin fragments also provides evidence for a gene duplication event. Preliminary studies also show that chromogranin may be degraded in the chromaffin granules by a calcium-dependent mechanism.

Original languageEnglish (US)
Pages (from-to)1645-1651
Number of pages7
JournalJournal of Biological Chemistry
Issue number3
StatePublished - Jan 1 1985

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Settleman, J., Fonseca, R., Nolan, J., & Angeletti, R. H. (1985). Relationship of multiple forms of chromogranin. Journal of Biological Chemistry, 260(3), 1645-1651.