Linked Life Data

9299521

Source:http://linkedlifedata.com/resource/pubmed/id/9299521

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-10-16
pubmed:abstractText
The complete amino acid sequence of the Rapana thomasiana hemocyanin N-terminal functional unit Rta was determined by direct sequencing and matrix-assisted laser desorption ionization mass spectrometry of the protein and peptides obtained by cleavage with EndoLysC proteinase, TPCK-trypsin and cyanogen bromide. The single polypeptide chain consists of 407 residues. This is the first report on the primary structure of a dioxygen-binding unit from a marine gastropod hemocyanin and of an N-terminal domain from a molluscan dioxygen carrier. Comparison with the sequences of other molluscan hemocyanin functional units shows an average identity of 48 +/- 5 %. Inspection of the Rta sequence revealed residues 27 and 250 as carbohydrate attachment sites. Conclusions about the molecular evolution of the molluscan hemocyanin dioxygen-binding functional units are made.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 1997 Academic Press.
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
238
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
403-10
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Complete amino acid sequence of dioxygen-binding functional unit of the Rapana thomasiana hemocyanin.
pubmed:affiliation
Abteilung für Physikalische Biochemie, Physiologisch-chemisches Institut der Universität Tübingen, Hoppe-Seyler-Str. 4, Tübingen, D-72076, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't