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Heat treated myosin does not bind ATPase ‐ inhibiting antibodies
Author(s) -
GröschelStewart Ute,
Christian AnnaLuise,
Mestan Jürgen
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203021
Subject(s) - myosin , polyclonal antibodies , antibody , myosin head , atpase , myosin atpase , microbiology and biotechnology , chemistry , blot , biochemistry , monoclonal antibody , myosin light chain kinase , biology , enzyme , immunology , gene
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 Ca2+‐activated myosin ATPase. Absorption of the antibodies with native myosin abolishes these reactions. Heat treatment of myosin for 2h at 40°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.