Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1995-6-30
pubmed:databankReference
pubmed:abstractText
A new lectin was purified from tubers of Arum maculatum L. by affinity chromatography on immobilized asialofetuin. Although this lectin is also retained on mannose-Sepharose 4B, under the appropriate conditions free mannose is a poor inhibitor of its agglutination activity. Pure preparations of the Arum lectin apparently yielded a single polypeptide band of approximately 12 kD upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. However, N-terminal sequencing of the purified protein combined with molecular cloning of the lectin have shown that the lectin is composed of two different 12-kD lectin subunits that are synthesized on a single large precursor translated from an mRNA of approximately 1400 nucleotides. Lectins with similar properties were also isolated from the Araceae species Colocasia esculenta (L.) Schott, Xanthosoma sagittifolium (L.) Schott, and Dieffenbachia sequina Schott. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration of the different Araceae lectins have shown that they are tetrameric proteins composed of lectin subunits of 12 to 14 kD. Interestingly, these lectins are the most prominent proteins in the tuber tissue. Evidence is presented that a previously described major storage protein of Colocasia tubers corresponds to the lectin.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-1329650, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-1375915, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-1394291, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-16664923, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-16665736, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-1718752, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-2350177, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-2461112, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-2463783, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-3758061, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-7680268, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-7873928, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-8106012, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-8223549, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-8251188, http://linkedlifedata.com/resource/pubmed/commentcorrection/7770523-942051
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
107
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1147-58
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The major tuber storage protein of araceae species is a lectin. Characterization and molecular cloning of the lectin from Arum maculatum L.
pubmed:affiliation
Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Belgium.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't