Linked Life Data

2775529

Source:http://linkedlifedata.com/resource/pubmed/id/2775529

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4-5
pubmed:dateCreated
1989-10-13
pubmed:abstractText
Monoclonal antibodies (mAbs) directed against porcine splenocyte phytohemagglutinin receptor glycoproteins were produced in BALB/c mice. Three antibody-producing, stable hybridomas were cloned and expanded in the peritoneal cavity of BALB/c mice. The mAbs (A7, B1, and H3) were purified and belong to the IgG2 subclass of immunoglobulins (kappa light chain). Each 125I-labeled mAb bound to purified porcine splenocytes with an (apparent) affinity KA congruent to 10(8) M-1 (Scatchard analysis). The number of (apparent) binding sites was 5 x 10(4) sites/cell in the case of B1 and H3, and approximately 15 x 10(4) sites/cell for A7. Immunoprecipitation experiments showed that the three mAbs recognized a single antigenic protein of Mr 80 kilodaltons (gp80). In addition, each mAb recognized a different epitope of gp80, as observed by Western blot analyses. Assessment of the relative ability of anti-gp80 mAbs to stimulate porcine splenocytes as determined by [3H]thymidine incorporation showed weak (A7 and B1) or no (H3) mitogenic activity. Cross-linked anti-gp80 mAbs were not mitogenic, except in the case of B1. In contrast, each anti-gp80 mAb (cross-linked or untreated) showed synergistic mitogenic properties when used in combination with a suboptimal concentration of phytohemagglutinin. The mechanism involved in this synergistic effect is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0829-8211
pubmed:author
pubmed:issnType
Print
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
224-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Properties of three monoclonal antibodies that recognize an 80-kDa phytohemagglutinin-binding glycoprotein from porcine lymphocytes.
pubmed:affiliation
Department of Biochemistry (Faculty of Medicine), University of Sherbrooke, Que., Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't