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Heat-treated myosin does not bind ATPase--inhibiting antibodies
- 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.
- Subjects :
- Protein Denaturation
Myosin light-chain kinase
Hot Temperature
Myosin ATPase
Protein Conformation
ATPase
Clinical Biochemistry
Blotting, Western
Enzyme-Linked Immunosorbent Assay
macromolecular substances
Myosins
Biochemistry
Antibodies
Antigen-Antibody Reactions
Myosin head
Adenosine Triphosphate
Western blot
Myosin
Genetics
medicine
Animals
Molecular Biology
Immunosorbent Techniques
biology
medicine.diagnostic_test
Cell Biology
Molecular biology
Peptide Fragments
Blot
Polyclonal antibodies
Muscle Fibers, Fast-Twitch
biology.protein
Chickens
Subjects
Details
- ISSN :
- 10399712
- Volume :
- 42
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Biochemistry and molecular biology international
- Accession number :
- edsair.doi.dedup.....0a36df58085525d78a541de4af8a4f90