NADH: (acceptor) oxidoreductase from bovine adrenal medulla chromaffin granules

Sam Zaremba, Ruth Hogue-Angeletti

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

The NADH:(acceptor) oxidoreductase from membranes of bovine adrenal medulla chromaffin granules has been purified by column chromatography. After solubilization of the membranes with emulphogen, a nonionic detergent, the enzyme was purified by dye-ligand chromatography and gel filtration. The oxidoreductase appeared essentially homogeneous on two gel electrophoretic systems. On polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, the enzyme revealed a dimeric structure with a combined molecular weight of about 55,000. The enzyme eluted as a detergent-lipid-protein aggregate with a Stoke's radius of 43 Å on gel filtration columns in the presence of emulphogen. The amino acid composition of the oxidoreductase was found to be distinct from that of similar enzymes from other organelles. Topographical experiments indicated that the enzyme is a transmembrane protein.

Original languageEnglish (US)
Pages (from-to)297-305
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume219
Issue number2
DOIs
StatePublished - Dec 1982

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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