Linked Life Data

16766219

Source:http://linkedlifedata.com/resource/pubmed/id/16766219

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2006-8-7
pubmed:abstractText
The extracellular hemoglobin of the lugworm Arenicola marina which inhabits on the intertidal area, a sulfide-rich environment, comprises eight globin chains previously determined by mass spectrometry. We have cloned and sequenced five of the globin components. The deduced amino-acid sequences exhibit an extracellular signal peptide and two cysteine residues involved in an internal disulfide bond. The molecular weights calculated from the globin primary structures obtained from complete cDNA sequences are in good agreement with the mass spectrometry values obtained with the native hemoglobin. Phylogenetic analysis has allowed assigning the five A. marina sequences to the different globin sub-families. Two of the globins were found to be A2 globin chains lacking the cysteine residues proposed to be involved in the binding of hydrogen sulfide by such hemoglobin. We discuss the unusual absence of these cysteines in the light of their invariant occurrence in the A2 subfamily of hemoglobins from annelids inhabiting sulfide-rich environments.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1096-4959
pubmed:author
pubmed:issnType
Print
pubmed:volume
144
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
319-25
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
The multigenic family of the extracellular hemoglobin from the annelid polychaete Arenicola marina.
pubmed:affiliation
Equipe Ecophysiologie: Adaptation et Evolution Moléculaires, UPMC, CNRS UMR 7144, Station Biologique, BP 74, 29682 Roscoff cedex, France. chabasse@sb-roscoff.fr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't