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Labelling and immunoprecipitation of thyroid microsomal antigen
Author(s) -
Kajita Y.,
Morgan D.,
Parkes A.B.,
Rees Smith B.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81271-0
Subject(s) - immunoprecipitation , microsome , antigen , biochemistry , chemistry , antibody , gel electrophoresis , microbiology and biotechnology , lectin , covalent bond , biology , enzyme , immunology , organic chemistry , gene
Human thyroid microsomes have been solubilized, labelled with 125 I, immunoprecipitated with microsomal antibody and analysed by gel electrophoresis. The analysis indicated that two peptides of relative molecular masses 108 and 118 kDa, under reducing conditions, were specifically immunoprecipitated by microsomal antibody. Similar values were obtained under non‐reducing conditions indicating that the two peptides were not linked by disulphide bridges to each other or to different peptides. These results suggest that the microsomal antigen contains two components which may be linked by non‐covalent bonds to form a single protein of 230 kDa. Studies with lectin affinity columns suggested that the antigen was glycosylated.