Heat-treated myosin does not bind ATPase--inhibiting antibodies

Biochem Mol Biol Int. 1997 Jul;42(3):611-9. doi: 10.1080/15216549700203021.

Abstract

Polyclonal antibodies to native chicken pectoral fast-twitch myosin are directed to all subfragments of the molecule (S1, S2 and LMM), as seen in the ELISA and Western blotting techniques. The antibodies inhibit the Ca(2+)-activated myosin ATPase. Absorption of the antibodies with native myosin abolishes these reactions. Heat treatment of myosin for 2h at 40 degrees C will inactivate myosin ATPase and alter its antibody binding pattern: the binding of antibodies to the rod fractions is reduced, that to the globular head (S1) completely abolished. Thus, these antibodies are useful as sensitive probes for the structural integrity of the myosin head.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Antibodies / metabolism*
  • Antigen-Antibody Reactions
  • Blotting, Western
  • Chickens
  • Enzyme-Linked Immunosorbent Assay
  • Hot Temperature*
  • Immunosorbent Techniques
  • Muscle Fibers, Fast-Twitch / chemistry
  • Myosins / antagonists & inhibitors*
  • Myosins / chemistry
  • Myosins / immunology
  • Myosins / metabolism*
  • Peptide Fragments / immunology
  • Protein Conformation
  • Protein Denaturation

Substances

  • Antibodies
  • Peptide Fragments
  • Adenosine Triphosphate
  • Myosins