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Identification of p70 and p80 Associations With Class II MHC Molecules and I i
Author(s) -
Sorli Christopher H.,
Reisert Patricia S.,
Humphreys Robert E.,
Welch William J.
Publication year - 1990
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/ajh.2830350304
Subject(s) - immunoprecipitation , methionine , mhc class i , gel electrophoresis , chemistry , monoclonal antibody , antigen , disulfide bond , major histocompatibility complex , biochemistry , microbiology and biotechnology , biology , genetics , amino acid , gene , antibody
Two proteins, p70 and p80, were found in chemically crosslinked complexes with class II MHC molecules and I i after 3–12 hr labelings with [ 35 S]methionine. Two‐dimensional, nonreduced/reduced SDS gel electrophoresis of immunoprecipitated complexes revealed 1) endogenous disulfide linkages between I i ‐I i and I i ‐p70 and 2) chemically crosslinked, nearest neighbors of α‐β, α‐I i , I i ‐p70, and α‐p80. Although such nearest neighbors within multimeric complexes were identified as dimers in nonreduced/reduced 2D gels, stoichiometries could not be determined in the high molecular weight complex(es), which included α, β, I i , p70, and p80, and were not separated in the first dimension. p80 was not the chondroitin‐sulfate form of I i (I i ‐CS) because it was not electrophoretically heterogeneous and was not sensitive to chondroitinase ABC. p70 was not hsp72/74 detected with C92 or N27 mAbs, and p80 was not BiP detected with its respective mAb. While only these two proteins associated prominently with class II MHC antigens and I i late after synthesis, their functions are unknown.
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