Linked Life Data

3772107

Source:http://linkedlifedata.com/resource/pubmed/id/3772107

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1986-11-24
pubmed:abstractText
A number of chemical disruption agents were assessed for their ability to dissociate HBsAg:anti-HBs immune complexes and to release both the antibody and antigen component in immunologically active forms. The most appropriate reagent was 0.1 M diethylamine which could elute up to 81% of anti-HBs antibody bound to solid-phase HBsAg and retained 93% of its antigen-combining activity. Complexes formed at various degrees of antigen excess and pre-exposed to 0.1 M diethylamine at room temperature for 18 h before ultracentrifugation on sucrose density gradients were effectively dissociated. The released antibody and antigen banded at their expected densities. However, the affinity of the isolated antibody for the detergent-solubilized polypeptide complex from purified HBsAg (gp30/p25) and cyclical peptides representing amino acids 124-137 and 139-147 of HBsAg were found to be considerably lower than that of the original pooled anti-HBs immunoglobulin used to form the immune complexes. These results suggest that the highest affinity antibody subpopulation may not be completely dissociated from the complex. Care should thus be exercised in the interpretation of the significance of the observed affinity of the antibody isolated by this and other similar dissociation procedures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-1759
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
93
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29-36
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
HBsAg: anti-HBs immune complexes. A method for separating the constituent components and assessment of the affinity of the antibody.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't