Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-9-29
pubmed:abstractText
The heparin-binding lectin, Anadarin MS, from the plasma of the marine clam Anadara granosa is purified through affinity chromatography on heparin-Sepharose 4B followed by gel filtration on a Sepharose 6B column. The purified lectin is a pentameric protein of native M(r) 300 kDa and is composed of identical subunits of 60 kDa. The pI value of this Ca(2+)-dependent lectin is 6.2. Anadarin MS agglutinates normal rabbit erythrocytes but not that of human. Aspartic acid, glutamic acid, histidine and glycine are the predominant amino acids. Unlike other reported heparin-binding lectins, Anadarin MS exhibits a unique and strict specificity for iduronic acid containing glycosaminoglycans. This lectin agglutinates infective promastigotes of Leishmania donovani exclusively and can therefore be used as a novel biochemical surface marker for this parasite.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
203
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
36-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Purification and partial characterization of a heparin-binding lectin from the marine clam Anadara granosa.
pubmed:affiliation
Department of Marine Science, University of Calcutta, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't