Monoclonal antibody ALD-58 reacted specifically with slow myosin and demonstrated immunological heterogeneity of myosins in type 1 skeletal muscle fibers.
This preclinical study demonstrates the immunological heterogeneity of myosins within histochemically identified type 1 skeletal muscle fibers using a novel monoclonal antibody.
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.
Shafiq et al. (Fri,) conducted a other in Skeletal muscle fibers. Monoclonal antibody ALD-58 was evaluated on Reactivity against different myosins. Monoclonal antibody ALD-58 reacted specifically with slow myosin and demonstrated immunological heterogeneity of myosins in type 1 skeletal muscle fibers.