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Immunochemical probing of the N-terminus of the myosin heavy chain
The reactivity of myosin subfragment 1 (S-1) towards site specific polyclonal anti-N-terminus antibodies was examined in competitive ELISA titrations. Tryptic digestion of S-1 and specifically the cleavage at the 25/50K junction greatly increased the accessibility of the N-terminus region to the antibodies. The binding of actin to S-1 did not change significantly the reactivity of either tryptic or intact S-1 towards anti-N-terminus antibodies. These results suggest the interdependence of the N-terminus and 25/50K junction regions on S-1.
The reactivity of myosin subfragment 1 (S-1) towards site specific polyclonal anti-N-terminus antibodies was examined in competitive ELISA titrations. Tryptic digestion of S-1 and specifically the cleavage at the 25/50K junction greatly increased the accessibility of the N-terminus region to the antibodies. The binding of actin to S-1 did not change significantly the reactivity of either tryptic or intact S-1 towards anti-N-terminus antibodies. These results suggest the interdependence of the N-terminus and 25/50K junction regions on S-1.