AI Article Synopsis
- The study identifies a new glycoprotein, termed pX, that associates specifically with the cell surface DP class II antigens in activated immune cells but is absent in resting B lymphocytes and other cell types.
- pX is heavily glycosylated, with its molecular mass ranging from 38 kDa to 22 kDa, which reduces to 22 kDa after deglycosylation.
- The findings suggest that pX does not exhibit polymorphism and is independent of the polymorphic nature of DP class II antigens, as indicated by consistent patterns observed in various donors.
Article Abstract
Two-dimensional electrophoretic analysis (2D-PAGE) of cell surface human DP and DR class II antigens identified a glycoprotein, designated pX, that is associated at the cell surface with DP but not DR class II antigen in activated T, B and NK lymphocytes but not in resting B lymphocytes, Raji B lymphoma cells, activated thymic epithelial cells or activated monocytes. pX is a heavily glycosylated protein with an apparent molecular mass spanning between 38 kDa and 22 kDa, that is reduced, after deglycosylation with Endo-F, to 22 kDa. The pX structure appears nonpolymorphic and independent of DP polymorphism, as suggested by 2D-PAGE migrational pattern of 125I-labelled Endo-F deglycosylated DP immunoprecipitates from T cells blasts derived from four donors with different DP allotypes. The apparent absence of polymorphism of pX is further suggested by two-dimensional peptide mapping of a single spot derived from 2D-PAGE of 125I-labelled DP deglycosylated immunoprecipitates from two donors.
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| http://dx.doi.org/10.1016/0161-5890(95)00143-3 | DOI Listing |
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