Statements in which the resource exists as a subject.
PredicateObject
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
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: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