The isolated 21 kDa N-terminal fragment of myosin binds to actin in an ATP and ionic strength-dependent manner
- 29 April 1991
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1077 (3) , 308-315
- https://doi.org/10.1016/0167-4838(91)90545-b
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Antibody directed against the 142-148 sequence of the myosin heavy chain interferes with myosin-actin interactionBiochemistry, 1991
- Isolation and characterization of the N-terminal 23-kilodalton fragment of myosin subfragment 1Biochemistry, 1989
- Selective cleavage of skeletal myosin subfragment‐1 to form a 26 kDa peptide which shows ATP‐sensitive actin bindingFEBS Letters, 1989
- A novel methodology for analysis of cell distribution in chimeric mouse organs using a strain specific antibody.The Journal of cell biology, 1988
- Identification of polyphosphate recognition sites communicating with the actin sites on the skeletal myosin subfragment-1 heavy chainBiochemistry, 1986
- Characterization of the isolated 20 kDa and 50 kDa fragments of the myosin headBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Fluorescence of fluorescein attached to myosin SH1 distinguishes the rigor state from the actin-myosin-nucleotide stateBiochemistry, 1984
- Mapping of actin-binding sites on the heavy chain of myosin subfragment 1Biochemistry, 1983
- Spectroscopic isolation of ES complexes of myosin subfragment-1 ATPase by fluorescence quenchingBiochemical and Biophysical Research Communications, 1982
- Photoaffinity labelling with an ATP analog of the N-terminal peptide of myosinBiochemical and Biophysical Research Communications, 1979