Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1986-5-14
|
pubmed:abstractText |
A lectin was purified from rice flour by aqueous extraction followed by precipitation by ammonium sulfate and affinity chromatography on p-aminobenzyl 2-acetamido-2-deoxy-1-thio-beta-D-glucoside-succinyl-aminohexylaminyl -Sepharose 4B. The molecular weight of the lectin is approximately 36,000, as determined by sedimentation-equilibrium analysis. It is a tetramer consisting of two different subunits (Mr = 12,000 +/- 1,000 and 9,000 +/- 1,000). Amino acid analysis indicated that the lectin contains very high proportions of half-cystine, glycine, and glutamic acid. All of the half-cystines are present as -S-S- bridges. The lectin agglutinates human A, B, AB, and O erythrocytes, rabbit erythrocytes, human leukocytes, and is mitogenic to human lymphocytes. The hemagglutinating activity of rice lectin is inhibited by 2-acetamido-2-deoxy-D-glucose, methyl 2-acetamido-2-deoxy-beta-D-glucoside, chitobiose, and chitotriose. N-Acetylneuraminic acid was a noninhibitor, but N-acetylneuramin-(2----3)-lactose showed weak inhibition. The agglutinating activity was also inhibited by various sialoglycoproteins. The immobilized rice-lectin bound glycophorin, alpha 1-acid glycoprotein, and fetuin. Asialoglycophorin, asialofetuin, ovomucoid, and human chorionic gonadotropin were bound only partially to the column.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ABO Blood-Group System,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/rice lectin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0008-6215
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
146
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
205-17
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:3955574-ABO Blood-Group System,
pubmed-meshheading:3955574-Amino Acids,
pubmed-meshheading:3955574-Animals,
pubmed-meshheading:3955574-Carbohydrates,
pubmed-meshheading:3955574-Chromatography, Affinity,
pubmed-meshheading:3955574-Erythrocytes,
pubmed-meshheading:3955574-Hemagglutination,
pubmed-meshheading:3955574-Hemagglutination Inhibition Tests,
pubmed-meshheading:3955574-Hemagglutination Tests,
pubmed-meshheading:3955574-Humans,
pubmed-meshheading:3955574-Lectins,
pubmed-meshheading:3955574-Lymphocyte Activation,
pubmed-meshheading:3955574-Molecular Weight,
pubmed-meshheading:3955574-Oryza sativa,
pubmed-meshheading:3955574-Plant Lectins,
pubmed-meshheading:3955574-Rabbits,
pubmed-meshheading:3955574-Structure-Activity Relationship
|
pubmed:year |
1986
|
pubmed:articleTitle |
Purification and saccharide-binding characteristics of a rice lectin.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|