Open AccessMolecular forms of soluble human t lymphocyte receptor for sheep erythrocytes in serum and saliva
Author(s) -
Itano Eiko N.,
Ono Mario A.,
Sumigawa Mari,
Longo Ieda M.,
Moura Nayla C.,
Mendes Nelson F.
Publication year - 1991
Publication title -
journal of clinical laboratory analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 50
eISSN - 1098-2825
pISSN - 0887-8013
DOI - 10.1002/jcla.1860050208
Subject(s) - saliva , sephadex , molecular mass , receptor , chemistry , lymphocyte , immunoprecipitation , microbiology and biotechnology , blood proteins , immunoelectrophoresis , serum albumin , albumin , biochemistry , antigen , biology , immunology , gene , enzyme
Using a specific serum anti‐soluble T lymphocytes receptor for sheep erythrocytes (E) and SDS‐PAGE, we detected radioactive bands of molecular weight 58,000 in immunoprecipitates of supernatant of heated human lymphocytes (SHL), in the supernatant of PHA stimulated lymphocyte cultures (SLC), normal human serum (NHS), and serum from cancer and uremia patients, labelled with 131 I. By Sephadex G‐200 chromatography, in addition to this fraction, we detected molecules of molecular weight higher than 150,000 which interact with the anti‐soluble receptor serum (anti‐Rs), in serum from cancer and uremia patients. These molecules were detected in NHS or SHL after concentration or by prolonged exposure of SDS‐PAGE with some labelled and immunoprecipitated SHL samples. The soluble receptors of molecular weights 58,000 (Rs1) and more than 150,000 (Rs2) were fully identical when analyzed by immunodiffusion with anti‐Rs serum. When submitted to immunoelectrophoresis, Rs1 showed electrophoretic migration similar to that of albumin, while Rs2 showed a pattern close to that of alpha2‐globulin. However, Rs2 did not show antigenic relationship with IgM and was not an immune complex with IgG. Even though the presence of Rs in human saliva has not yet been reported, molecules that interact with anti‐Rs serum have been detected in human saliva and are fully identical to molecules found in supernatant of heated human T lymphocytes and NHS. The Rs molecules present in human saliva have a molecular weight and electrophoretic migration similar to those of Rs 1 from SLC and from human serum and have no antigenic relationship with human albumin.