Source:http://linkedlifedata.com/resource/pubmed/id/16662262
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2010-6-29
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pubmed:abstractText |
Soybean (Glycine max L.) seeds contain a galactose-binding protein which displays two activities: (a) an alpha-galactosidase activity and (b) a hemagglutinin activity. The alpha-galactosidase-hemagglutinin was purified to homogeneity by conventional protein purification procedures and also by affinity chromatography. This protein can be easily separated from soybean agglutinin, the N-acetyl-d-galactosamine-specific lectin in soybean. Further, these two agglutinins show no immunological relatedness. The alpha-galactosidase-hemagglutinin can be reversibly converted by pH changes from a tetrameric form which displays both enzymic and hemagglutinin activities to a monomeric form which displays enzymic activity only. Although both the monomeric and tetrameric forms are enzymically active, they display different pH optima and carbohydrate specificities.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16662262-13578996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16662262-16660894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16662262-16661250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16662262-19253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16662262-212437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16662262-5948568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16662262-6265439
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pubmed:language |
eng
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pubmed:journal | |
pubmed:status |
PubMed-not-MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0032-0889
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
69
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
628-31
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pubmed:dateRevised |
2010-9-15
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pubmed:year |
1982
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pubmed:articleTitle |
An alpha-Galactosidase with Hemagglutinin Properties from Soybean Seeds.
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pubmed:affiliation |
Department of Biochemistry, University of California, Riverside, California 92521.
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pubmed:publicationType |
Journal Article
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