Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-6-29
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.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Mar
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
69
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
628-31
pubmed:dateRevised
2010-9-15
pubmed:year
1982
pubmed:articleTitle
An alpha-Galactosidase with Hemagglutinin Properties from Soybean Seeds.
pubmed:affiliation
Department of Biochemistry, University of California, Riverside, California 92521.
pubmed:publicationType
Journal Article