Linked Life Data

6084639

Source:http://linkedlifedata.com/resource/pubmed/id/6084639

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1985-4-18
pubmed:abstractText
Five monoclonal antibodies (A7, B24, I14, L12, and M2) recognizing different epitopes of the human natural IFN-gamma were prepared by immunizing BALB/c mice with a highly purified human natural IFN-gamma preparation (10(7) U/mg). All five antibodies had high IFN-gamma-binding activity but exhibited differential IFN-gamma-neutralizing activities. Furthermore, none of them neutralized the antiviral activity exhibited by either IFN-alpha or IFN-beta preparations, indicating thus their specificity for IFN-gamma. The A7, L12, M2, and I14 monoclonal antibodies, but not the B24, blocked the augmentation of natural killer cytotoxicity, mediated by peripheral blood monocyte-depleted lymphocytes, by Escherichia coli-derived IFN-gamma or natural IFN-gamma but not by IFN-alpha 2. All five monoclonal antibodies precipitated an identical molecular complex containing two major protein components with molecular weights of 20,000 (20 kD) and 25,000 (25 kD) and two minor components with molecular weights of 17,000 (17 kD) and 45,000 (45 kD). Treatment of the immunoprecipitated IFN-gamma molecule with endoglycosylase F led to a stepwise removal of the carbohydrate portions on both the 25 and 20 kD chains, which resulted in the appearance of both 16 kD and 18 kD chains. The hereby reported monoclonal anti-IFN-gamma antibodies will prove useful as probes for purification and for rapid assay of human IFN-gamma molecule.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0272-457X
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
321-32
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Preparation and characterization of monoclonal antibodies directed at epitopes of human IFN-gamma.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't