HEAT-TREATED MYOSIN DOES NOT BIND ATPASE - INHIBITING ANTIBODIES

Citation
U. Groschelstewart et al., HEAT-TREATED MYOSIN DOES NOT BIND ATPASE - INHIBITING ANTIBODIES, Biochemistry and molecular biology international, 42(3), 1997, pp. 611-619
Citations number
22
ISSN journal
10399712
Volume
42
Issue
3
Year of publication
1997
Pages
611 - 619
Database
ISI
SICI code
1039-9712(1997)42:3<611:HMDNBA>2.0.ZU;2-0
Abstract
Polyclonal antibodies to native chicken pectoral fast-twitch myosin ar e directed to all subfragments of the molecule (S-1, S-2 and LMM), as seen in the ELISA and Western blotting techniques. The antibodies inhi bit the Ca2+-activated myosin ATPase. Absorption of the antibodies wit h native myosin abolishes these reactions. Heat treatment of myosin fo r 2h at 40 degrees C will inactivate myosin ATPase and alter its antib ody binding pattern: the binding of antibodies to the rod fractions is reduced, that to the globular head (S-1) completely abolished. Thus, these antibodies are useful as sensitive probes for the structural int egrity of the myosin head.