The proteolytic substructure of light meromyosin. Localization of a region responsible for the low ionic strength insolubility of myosin.
Open Access
- 1 November 1983
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 258 (21) , 13213-13220
- https://doi.org/10.1016/s0021-9258(17)44103-2
Abstract
No abstract availableThis publication has 33 references indexed in Scilit:
- Proximity of alkali light chains to 27K domain of the heavy chain in myosin subfragment 1Biochemical and Biophysical Research Communications, 1981
- Localization of the reactive trinitrophenylated lysyl residue of myosin ATPase site in the NH2‐terminal (27 k domain) of S1 heavy chainFEBS Letters, 1980
- Photoaffinity labelling with an ATP analog of the N-terminal peptide of myosinBiochemical and Biophysical Research Communications, 1979
- Isolation and physico-chemical properties of a high molecular weight subfragment-2 of myosinJournal of Molecular Biology, 1978
- Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibilityJournal of Molecular Biology, 1977
- Thermal transitions of myosin and its helical fragments. Regions of structural instability in the myosin moleculeBiochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Substructure of the myosin moleculeJournal of Molecular Biology, 1969
- Studies on proteins and protein complexes of muscle by means of proteolysis: V. Fragmentation of light meromyosin by trypsinJournal of Molecular Biology, 1968
- Light meromyosin fraction I: A helical molecule from myosinJournal of Molecular Biology, 1960