Linked Life Data

3082650

Source:http://linkedlifedata.com/resource/pubmed/id/3082650

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1986-5-12
pubmed:abstractText
The internalization and intracellular processing of monoclonal antibody to immunoglobulin mu heavy chain (Mamu) have been investigated in two human Burkitt lymphoma cell lines (Ramos and Raji), in a human B cell lymphoma and in normal human peripheral blood B cells. In addition to the degradation of 125I-labeled Mamu to trichloroacetic acid (TCA) soluble material, a distinct pattern of larger 125I-Mamu fragments was detected in all sources of B cells tested. The particular fragmentation pattern, as revealed by sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis, involved the cleavage of both peptide bonds and disulfide bridges. This type of antibody fragmentation appeared to be a selective mechanism associated with sIgM, as no other degradation than that leading to TCA-soluble material could be detected after the internalization and degradation of radiolabeled monoclonal antibodies towards a variety of non-Ig B cell surface receptors. Three fragments of 125I-Mamu degradation were also detected in the supernatant of Ramos cells, implying that the recycling and exocytosis of certain 125I-Mamu fragments also took place.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-2980
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
286-91
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Internalization and processing of antibodies to surface antigens on human B cells. Monoclonal anti-IgM antibodies are processed differently than monoclonal antibodies towards non-Ig surface receptors.
pubmed:publicationType
Journal Article