The interaction of arsenite with the molybdenum center of chicken liver xanthine dehydrogenase.

Published

Journal Article

Inactivation of chicken liver xanthine dehydrogenase by arsenite is reflected in the molybdenum electron paramagnetic resonance signal at g = 1.97. The arsenite spectrum shows additional splittings and considerable broadening yet remains comparable to the native in total intensity. Further subtle alterations of the molybdenum signal of arsenite-treated enzyme are seen in the presence of purine-type substrates or inhibitors.

Full Text

Duke Authors

Cited Authors

  • Johnson, JL; Rajagopalan, KV

Published Date

  • 1978

Published In

Volume / Issue

  • 8 / 5

Start / End Page

  • 439 - 444

PubMed ID

  • 210844

Pubmed Central ID

  • 210844

International Standard Serial Number (ISSN)

  • 0006-3061

Language

  • eng

Conference Location

  • United States