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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-10-1
pubmed:abstractText
Three rhamnose-binding lectins were purified from the roe of Osmerus eperlanus mordax (olive rainbow smelt) by affinity chromatography and ion-exchange chromatography. The apparent molecular weights of Osmerus eperlanus mordax lectin (OML) -1, -2 and -3 were 25000, 32000 and 26000, respectively, on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions. On native PAGE, these three lectins showed different migration patterns (Rm value; 0.37, 0.53 and 0.66, respectively). OMLs agglutinated rabbit and human type B erythrocytes and sarcoma 180 cells, but not human type A and O erythrocytes and AH109A cells. The most effective monosaccharide inhibitor was L-rhamnose. L-Mannose and D-galactose were also good inhibitors. Furthermore, OML-induced hemagglutination was inhibited more strongly by melibiose or raffinose rather than lactose or lactulose. Therefore, OMLs are L-rhamnose/alpha-D-galactosyl type lectins. OMLs did not require a detergent, when extracted from crude material, and Ca2+, Mg2+, EDTA and dithiothreitol were not necessary for the OML-induced hemagglutination activities. The OMLs had similar N-terminal amino acid sequences.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0918-6158
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
239-43
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8364467-Amino Acid Sequence, pubmed-meshheading:8364467-Animals, pubmed-meshheading:8364467-Carbohydrates, pubmed-meshheading:8364467-Chromatography, Affinity, pubmed-meshheading:8364467-Chromatography, Ion Exchange, pubmed-meshheading:8364467-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8364467-Fishes, pubmed-meshheading:8364467-Hemagglutination Inhibition Tests, pubmed-meshheading:8364467-Hemagglutination Tests, pubmed-meshheading:8364467-Hydrolysis, pubmed-meshheading:8364467-Lectins, pubmed-meshheading:8364467-Molecular Sequence Data, pubmed-meshheading:8364467-Molecular Weight, pubmed-meshheading:8364467-Ovum, pubmed-meshheading:8364467-Rabbits, pubmed-meshheading:8364467-Rhamnose, pubmed-meshheading:8364467-Sarcoma 180, pubmed-meshheading:8364467-Tumor Cells, Cultured
pubmed:year
1993
pubmed:articleTitle
Three rhamnose-binding lectins from Osmerus eperlanus mordax (olive rainbow smelt) roe.
pubmed:affiliation
Cancer Research Institute, Tohoku College of Pharmaceutical Sciences, Sendai, Japan.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't