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.
D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D000937:Antigen-Antibody Reactions; D015879:Myosin Subfragments; D009218:Myosins / Q000276:immunology / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding; D011817:Rabbits; D014357:Trypsin / Q000378:metabolism
D000199:Actins; D015879:Myosin Subfragments; D010446:Peptide Fragments; D014357:Trypsin; D009218:Myosins