Correlation of CD2 binding and functional properties of multimeric and monomeric lymphocyte function-associated antigen 3.
LFA-3 was purified with an intact (mLFA-3) or an enzymatically removed membrane-anchoring domain (sLFA-3). Gel filtration and sucrose gradient sedimentation showed sLFA-3 to be a single highly glycosylated polypeptide chain in solution, while mLFA-3 formed micelles of 8 LFA-3 monomers. 125I-mLFA-3 b...
المؤلفون الرئيسيون: | Dustin, M, Olive, D, Springer, T |
---|---|
التنسيق: | Journal article |
اللغة: | English |
منشور في: |
1989
|
مواد مشابهة
-
Purified lymphocyte function-associated antigen 3 binds to CD2 and mediates T lymphocyte adhesion.
حسب: Dustin, M, وآخرون
منشور في: (1987) -
Primary structure of lymphocyte function-associated antigen 3 (LFA-3). The ligand of the T lymphocyte CD2 glycoprotein.
حسب: Wallner, B, وآخرون
منشور في: (1987) -
Enteric pharmacokinetics of monomeric and multimeric camelid nanobody single-domain antibodies
حسب: Michelle Debatis, وآخرون
منشور في: (2023-01-01) -
Purified lymphocyte function-associated antigen-3 (LFA-3) activates human thymocytes via the CD2 pathway.
حسب: Denning, S, وآخرون
منشور في: (1988) -
Purified lymphocyte function-associated antigen-3 and T11 target structure are active in CD2-mediated T cell stimulation.
حسب: Tiefenthaler, G, وآخرون
منشور في: (1987)