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Albumin‐Immunoglobulin Complexes in Human Serum: Classification and Immunochemical Analysis
Author(s) -
EILAT D.,
FISCHEL R.,
ZLOTNICK A.
Publication year - 1981
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1981.tb00186.x
Subject(s) - albumin , immunoelectrophoresis , antibody , chemistry , serum albumin , polyclonal antibodies , covalent bond , biochemistry , bovine serum albumin , human serum albumin , affinity chromatography , immunoglobulin g , microbiology and biotechnology , chromatography , immunology , medicine , biology , enzyme , organic chemistry
A complex between serum albumin and immunoglobulins was observed on immunoelectrophoresis in six patients. Two patients with multiple myeloma had monoclonal IgA–albumin complexes; one of these complexes was formed by covalent bonds and the other by non‐covalent bonds. Four patients displayed non‐covalent IgG‐albumin complexes: of these, one had multiple myeloma, two had been treated with nitrofurantoin for prolonged periods, and one had diabetes mellitus. The IgG‐albumin complex of the last patient was subjected to a detailed immunochemical analysis. The albumin‐specific antibodies were isolated by affinity chromatography and analysed, using a sensitive tritium labelling technique. The antibodies were polyclonal, complexed with serum albumin through their Fab portion, and showed a high specificity for the human albumin as compared with bovine and rabbit albumins. The serum albumin of two patients displayed an abnormal behaviour in reduced SDS‐polyacrylamide gel electrophoresis (PAGE). The abnormal albumins had an apparent molecular weight of 52,000 and could read with rabbit anti‐human serum albumin like the normal protein. No abnormal albumin could be detected in 20 other patients' sera, including nitrofurantoin‐treated patients and normal controls. These findings suggest a possible role for an altered self‐component in the triggering of a specific autoimmune reaction.