Purification of membrane-bound dopamine β-monooxygenase from chromaffin granules

Relation to soluble dopamine β-monooxygenase

Emily P. Slater, Samuel Zaremba, Ruth A. Hogue-Angeletti

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Membrane-bound dopamine β-monooxygenase (MDBH) has been solubilized using emulphogen, a nonionic detergent, and purified by a single-step anion-exchange chromatography on DEAE-cellulose. Reduced and denatured MDBH has a molecular weight of approximately 75,000. The unreduced MDBH has a molecular weight twice that size. MDBH and SDBH (soluble dopamine β-monooxygenase) possess many similar features. Using antiserum to SDBH, the two proteins show a reaction of identity in immunodiffusion assays. Their chromatographic, electrophoretic, and molecular weight characteristics are also very similar. Although the amino acid compositions of MDBH and SDBH were not dissimilar, the MDBH composition had a higher content of certain amino acids, particularly hydrophobic ones. Despite the remarkable likeness of MDBH and SDBH demonstrated above and by analytical peptide maps, peptides can be detected in MDBH which are not found in SDBH.

Original languageEnglish (US)
Pages (from-to)288-296
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume211
Issue number1
DOIs
StatePublished - Oct 1 1981
Externally publishedYes

Fingerprint

Chromaffin Granules
Mixed Function Oxygenases
Purification
Dopamine
Molecular Weight
Molecular weight
Membranes
Amino Acids
DEAE-Cellulose Chromatography
DEAE-Cellulose
Peptides
Immunodiffusion
Chromatography
Chemical analysis
Detergents
Anions
Immune Sera
Assays
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Purification of membrane-bound dopamine β-monooxygenase from chromaffin granules : Relation to soluble dopamine β-monooxygenase. / Slater, Emily P.; Zaremba, Samuel; Hogue-Angeletti, Ruth A.

In: Archives of Biochemistry and Biophysics, Vol. 211, No. 1, 01.10.1981, p. 288-296.

Research output: Contribution to journalArticle

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