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

Authors :
Jürgen Mestan
Ute Gröschel‐Stewart
Anna‐Luise Christian
Source :
Biochemistry and molecular biology international. 42(3)
Publication Year :
1997

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.

Details

ISSN :
10399712
Volume :
42
Issue :
3
Database :
OpenAIRE
Journal :
Biochemistry and molecular biology international
Accession number :
edsair.doi.dedup.....0a36df58085525d78a541de4af8a4f90