Linked Life Data

21802403

Source:http://linkedlifedata.com/resource/pubmed/id/21802403

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2011-9-13
pubmed:abstractText
Hephaestin is a multicopper ferroxidase involved in iron absorption in the small intestine. Expressed mainly on the basolateral surface of duodenal enterocytes, hephaestin facilitates the export of iron from the intestinal epithelium into blood by oxidizing Fe(2+) into Fe(3+), the only form of iron bound by the plasma protein transferrin. Structurally, the human hephaestin ectodomain is predicted to resemble ceruloplasmin, the major multicopper oxidase in blood. In addition to its ferroxidase activity, ceruloplasmin was reported to oxidize a wide range of organic compounds including a group of physiologically relevant substrates (biogenic amines). To study oxidation of organic substrates, the human hephaestin ectodomain was expressed in Pichia pastoris. The purified recombinant hephaestin has an average copper content of 4.2 copper atoms per molecule. The K(m) for Fe(2+) of hephaestin was determined to be 3.2?M which is consistent with the K(m) values for other multicopper ferroxidases. In addition, the K(m) values of hephaestin for such organic substrates as p-phenylenediamine and o-dianisidine are close to values determined for ceruloplasmin. However, in contrast to ceruloplasmin, hephaestin was incapable of direct oxidation of adrenaline and dopamine implying a difference in biological substrate specificities between these two homologous ferroxidases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1096-0384
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
514
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
50-6
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Oxidation of organic and biogenic amines by recombinant human hephaestin expressed in Pichia pastoris.
pubmed:affiliation
Department of Biochemistry and Molecular Biology and Centre for Blood Research, University of British Columbia, Vancouver, BC, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't