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Cross‐reactivity of an antineurofilament antibody with a troponin‐T isoform
Author(s) -
Takagi Michito,
TakanoOhmuro Hiromi,
Nakamura Toshitaka,
Kawahara Hajime,
Shimizu Teruo,
Obinata Takashi,
Kohama Kazuhiro
Publication year - 1989
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880121007
Subject(s) - gene isoform , myofibril , monoclonal antibody , skeletal muscle , microbiology and biotechnology , troponin , troponin t , troponin c , chemistry , antibody , western blot , biochemistry , actin , myoglobin , biology , medicine , anatomy , immunology , myocardial infarction , gene
Abstract Histochemical examination has revealed that a monoclonal antibody raised against the 200‐kilodalton (kd) subunit of neurofilament reacts not only with neural tissue but with type 1 and type 2C fibers of skeletal muscle. To identify the cross‐reactive substance(s), rat soleus muscle, which includes type 1 and type 2C fibers, was separated into a soluble fraction and an insoluble myofibrillar fraction. Western blot analysis demonstrated that the antibody reacted with 30‐kd and 36‐kd polypeptides in the soluble fraction and with a 38‐kd polypeptide in the insoluble fraction. We isolated a fraction that contained the 38‐kd polypeptide from the insoluble fraction. The material in this fraction bound to F‐actin. Two‐dimensional electrophoresis of the fraction showed that the 38‐kd polypeptide was part of the group of isoforms of troponin‐T, which was identified by a monoclonal antibody developed against troponin‐T. Thus, we conclude that this antineurofilament antibody recognizes one of the isoforms of troponin‐T in type 1 and type 2C fibers.