Premium
Heterogeneity of type 1 skeletal muscle fibers revealed by monoclonal antibody to slow myosin
Author(s) -
Shafiq Saiyid A.,
Shimizu Teruo,
Fischman Donald A.
Publication year - 1984
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.880070507
Subject(s) - myosin , skeletal muscle , monoclonal antibody , chemistry , radioimmunoassay , immunofluorescence , microbiology and biotechnology , antibody , biology , biochemistry , anatomy , immunology
Monoclonal antibodies (McAbs) were generated against slow myosin from the chicken anterior latissimus dorsi (ALD) muscle and their reactivity was checked against fast (pectoralis), slow (ALD), cardiac (ventricular), and smooth (gizzard) myosins by radioimmunoassay (RIA), immunoautoradiography (immunoblots), and indirect immunofluorescence techniques. In RIAs, the McAb (ALD‐58) described in this article reacted specifically with slow myosin, with only a weak cross‐reactivity to cardiac myosin. In immunoblots against whole muscle homogenates and purified myosins, it bound selectively to the 200 Kd myosin heavy chain band. The ALD‐58 antibody stained the fibers of the ALD muscle uniformly but gave three grades of reactions (strong, weak, and negative), with histochemically identified type 1 fibers of sartorius and gastrocnemius muscles demonstrating the immunological heterogeneity of myosins in type 1 skeletal muscle fibers.