Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1982-9-17
pubmed:abstractText
Binding constants of monomers of seven BALB/c IgM, four BALB/c IgA, and one C57BL/6 IgA anti-alpha (1 leads to 6) dextran hybridoma antibodies with dextran B512 and with isomaltoheptaose were determined by affinity electrophoresis. Bindings constants to dextran range from 1.52 X 10(5) to 4.43 X 10(5) ml/g for the five IgA monomers and from 1.70 X 10(3) to 6.10 X 10(4) ml/g for the seven IgM monomers. Antibody monomers containing both specific and nonspecific (derived from the myeloma cell that was used to generate the hybridomas) light chains are shown to have association constants with dextran 6 to 30-fold lower than monomers containing only specific light chain, suggesting that the association of specific heavy chain with nonspecific light chain does not result in an anti-dextran combining site. Binding constants with isomaltoheptaose range from 1.45 X 10(4) to 7.01 X 10(4)/M for the IgA proteins and from 6.46 X 10(3) to 7.70 X 10(4)/M for the IgM proteins. The binding constants with dextran and with isomaltoheptaose, and the electrophoretic, immunochemical and idiotypic characteristics of the hybridoma proteins are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0161-5890
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
389-97
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Association constants of hybridoma antibodies specific for alpha (1 leads to 6) linked dextran determined by affinity electrophoresis.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.