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

Judith Nolan, Randi Fonseca, Ruth Hogue Angeletti

Research output: Contribution to journalArticle

8 Citations (Scopus)

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
StatePublished - 1985
Externally publishedYes

Fingerprint

Mixed Function Oxygenases
Dopamine
Monoclonal Antibodies
Chromaffin Granules
Immunization
Membranes
Peptides
Biosynthesis
Immune Sera
Epitopes
Antibodies
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A monoclonal antibody to dopamine β-monooxygenase : Detection of biosynthetic intermediates. / Nolan, Judith; Fonseca, Randi; Angeletti, Ruth Hogue.

In: Archives of Biochemistry and Biophysics, Vol. 240, No. 1, 1985, p. 257-264.

Research output: Contribution to journalArticle

Nolan, Judith ; Fonseca, Randi ; Angeletti, Ruth Hogue. / A monoclonal antibody to dopamine β-monooxygenase : Detection of biosynthetic intermediates. In: Archives of Biochemistry and Biophysics. 1985 ; Vol. 240, No. 1. pp. 257-264.
@article{5de6214512b14f0cab10572fa98edda6,
title = "A monoclonal antibody to dopamine β-monooxygenase: Detection of biosynthetic intermediates",
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.",
author = "Judith Nolan and Randi Fonseca and Angeletti, {Ruth Hogue}",
year = "1985",
doi = "10.1016/0003-9861(85)90031-1",
language = "English (US)",
volume = "240",
pages = "257--264",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - A monoclonal antibody to dopamine β-monooxygenase

T2 - Detection of biosynthetic intermediates

AU - Nolan, Judith

AU - Fonseca, Randi

AU - Angeletti, Ruth Hogue

PY - 1985

Y1 - 1985

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0021888597&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021888597&partnerID=8YFLogxK

U2 - 10.1016/0003-9861(85)90031-1

DO - 10.1016/0003-9861(85)90031-1

M3 - Article

C2 - 2409921

AN - SCOPUS:0021888597

VL - 240

SP - 257

EP - 264

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 1

ER -