Abstract:
:The biochemical behavior and peptide binding properties of a soluble form of the human class II DR4Dw4 molecule (PI-DR4Dw4) were compared to DR4Dw4 molecules containing the transmembrane and cytoplasmic domains that were purified both from B and transfected chinese hamster ovary cells. Recombinant and B cell-derived DR4Dw4 molecules bound monoclonal anti-DR4Dw4 antibodies with different affinities and varied in their stability in the presence of sodium dodecyl sulfate. The three forms of DR4Dw4 bound peptides with a similar apparent affinity constant, but soluble class II molecules bound up to ten times more peptide than DR4Dw4 containing a transmembrane region. Peptide binding kinetics for soluble DR4Dw4 molecules were 10-20 times faster than for the other two forms of DR4Dw4 molecules. Finally, soluble PI-DR4Dw4/peptide complexes were shown to stimulate T cell proliferation.
journal_name
Eur J Immunoljournal_title
European journal of immunologyauthors
Buelow R,Paborsky LR,van Schooten WC,Kummerehl TJ,Schreifels R,Marshall K,Mayer J,Rothbard JBdoi
10.1002/eji.1830230112subject
Has Abstractpub_date
1993-01-01 00:00:00pages
69-76issue
1eissn
0014-2980issn
1521-4141journal_volume
23pub_type
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