Purification and characterization of myosins from human and rabbit skeletal muscles by using specific monoclonal antibodies.
By using immunoaffinity column chromatography slow (I) and fast (IIA, IIB) myosins were isolated from human (vastus lateralis) and rabbit (tibialis anterior, psoas and conoidal bundle) skeletal muscles. The peptide pattern revealed that slow (I) and fast (IIA, IIB) myosin heavy chains are quite distinct, as are those from pure slow (conoidal bundle) and fast (psoas) rabbit skeletal muscles. Unlike Billeter et al. (1981) the authors observed that fast human myosins were always associated with a small amount of slow myosin light chains. The fast myosins (IIA, IIB) from rabbit tibialis anterior muscle did not appear very distinct and contained only fast myosin light chains. These myosins were different from the IIB myosin from the psoas muscle. Ten per cent of the fibres revealed histochemically as fast IIA also reacted with an anti-slow myosin antibody. The classical histochemical techniques appear inadequate to demonstrate the existing differences among fibre types, but the monoclonal antibodies hold promise.
D000818:Animals; D000911:Antibodies, Monoclonal; D002846:Chromatography, Affinity; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis* / Q000166:cytology; D015879:Myosin Subfragments; D009218:Myosins / Q000276:immunology / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000302:isolation & purification; D011817:Rabbits; D013045:Species Specificity
D000911:Antibodies, Monoclonal; D015879:Myosin Subfragments; D010446:Peptide Fragments; D009218:Myosins