Purification and properties of sulfite oxidase from human liver.

Journal Article (Journal Article)

Sulfite oxidase has been purified to near homogeneity from human liver. Properties of the molecule have been investigated and compared to those of the rat liver enzyme which has been isolated in a pure form. Both proteins exist as dimeric molecules with one molybdenum and one cytochrome b5-type heme per sub-unit. The human enzyme has a slightly larger subunit molecular weight (61,100 vs. 57,200 daltons) and is a more negatively charged molecule. Decreased reactivity of the human enzyme with various electron acceptors suggests the presence of nonfunctional molybdenum centers in a portion of the molecules isolated. Human liver sulfite oxidase cross-reacts strongly with antibody prepared against the rat liver enzyme. Human enzyme activity is precipitated by antibody at concentrations about twofold greater than required for comparable complexation of rat sulfite oxidase.

Full Text

Duke Authors

Cited Authors

  • Johnson, JL; Rajagopalan, KV

Published Date

  • September 1, 1976

Published In

Volume / Issue

  • 58 / 3

Start / End Page

  • 543 - 550

PubMed ID

  • 956383

Pubmed Central ID

  • PMC333211

International Standard Serial Number (ISSN)

  • 0021-9738

Digital Object Identifier (DOI)

  • 10.1172/JCI108499


  • eng

Conference Location

  • United States