Linked Life Data

1830789

Source:http://linkedlifedata.com/resource/pubmed/id/1830789

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-9-11
pubmed:abstractText
Binding specificities of calcium-dependent and -independent bovine IgM and IgG reactive with unsubstituted Sepharose 4B were determined by competitive binding assays. The binding of 125I-labeled calcium-dependent bovine IgM to unsubstituted Sepharose 4B was most effectively inhibited by lactose which was about 100 times more reactive than galactose and melibiose. Other inhibitors were much less potent. With 125I-labeled calcium-independent bovine IgM and IgG, on the other hand, lactose was as potent as galactose. Melibiose was about 10 times less potent than lactose and galactose, whereas other mono- and disaccharides were much less potent. From these findings, the combining site of calcium-dependent bovine IgM reactive with unsubstituted Sepharose 4B may be specific for lactose, whereas those of calcium-independent bovine IgM and IgG specific for galactose.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0916-7250
pubmed:author
pubmed:issnType
Print
pubmed:volume
53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
185-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Immunochemical specificities of the combining sites of bovine immunoglobulins reactive with sepharose 4B.
pubmed:affiliation
Department of Serology and Immunology, School of Medical Technology, Kitasato University, Kanagawa, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't