Isolation of the domain containing the molybdenum, iron-sulfur I, and iron-sulfur II centers of chicken liver xanthine dehydrogenase.

Published

Journal Article

Chicken liver xanthine dehydrogenase, like other xanthine-oxidizing enzymes, is a dimer of Mr = 150,000 subunits. Each subunit contains one molybdenum, one FAD, and two distinct Fe2S2 centers. Treatment with a number of proteases shows that the native enzyme subunit is cleaved at three distinct sites. However, the cleavage products can be separated only under denaturing conditions. Prolonged treatment with subtilisin at pH 10.1 has permitted the isolation of an Mr = 65,000 catalytically active fragment that is devoid of FAD but which contains the molybdenum and both types of iron-sulfur center. A model of the domain structure of the native enzyme is proposed.

Full Text

Duke Authors

Cited Authors

  • Coughlan, MP; Betcher-Lange, SL; Rajagopalan, KV

Published Date

  • November 10, 1979

Published In

Volume / Issue

  • 254 / 21

Start / End Page

  • 10694 - 10699

PubMed ID

  • 227849

Pubmed Central ID

  • 227849

International Standard Serial Number (ISSN)

  • 0021-9258

Language

  • eng

Conference Location

  • United States