A monoclonal antibody to dopamine β-monooxygenase: Detection of biosynthetic intermediates

Judith Nolan, Randi Fonseca, Ruth Hogue Angeletti

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

A monoclonal antibody to dopamine β-monooxygenase (DBH) has been produced by an in vitro immunization technique. This antibody has been found to react with an epitope common to both soluble DBH (SDBH) and membrane-bound DBH (MDBH). A single CNBr fragment contains this antigenic site. Examination of electrophoretograms of chromaffin granule membrane and lysate by the immunoblot procedure revealed additional complexity. A 58-KDa polypeptide in low abundance was stained which could not be detected with the polyclonal antiserum. Chemical deglycosylation of SDBH produces two new polypeptides of 67 and 58 KDa. The entirety of this data suggests that the 58-KDa band is an unglycosylated form of DBH, proteolytically cleaved after biosynthesis.

Original languageEnglish (US)
Pages (from-to)257-264
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume240
Issue number1
DOIs
Publication statusPublished - Jul 1985

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ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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