Isolation and identification of an α2subclass lymphotoxin (LT) subunit from the high-molecular-weight (complex) human LT class
- Author(s): Devlin, JJ
- Klostergaard, J
- Granger, GA
- et al.
Published Web Locationhttps://doi.org/10.1016/0008-8749(84)90163-1
The high-molecular-weight (MW) complex class (MW = ≥ 200,000) of lymphotoxin (LT) may be involved in the process of lymphocyte-mediated cytolysis. This LT class was produced by concanavalin A-stimulated human adenoid and tonsil lymphocytes in vitro and purified ~1000 fold by a scheme employing lectin affinity chromatography on concanavalin A-Sepharose, negative hydrophobic affinity chromatography on phenyl-Sepharose, and molecular sieving on Ultrogel AcA 44. A cell-lytic subunit, termed C-alpha toxin, was dissociated from this partially purified complex LT (Cx) preparation. The identification of C-alpha toxin as an α2LT form was established by its comigration with the α2LT form during native polyacrylamide gel electrophoresis (PAGE), molecular sieving, and isoelectricfocusing. In addition, C-alpha toxin was neutralized by antiserum raised against purified α2LT, and the latter was neutralized by antiserum raised against C-alpha toxin. Furthermore, preliminary evidence indicates that both α2LT and C-alpha toxin are composed of peptides with apparent MW of ~69,000. Additional data indicate the Cx LT form is composed of α2LT and other subunits. © 1984.
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