Actin-binding peptide obtained by the cyanogen bromide cleavage of the 20-kDa fragment of myosin subfragment-1.
Open Access
- 1 June 1985
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 260 (11) , 6723-6727
- https://doi.org/10.1016/s0021-9258(18)88839-1
Abstract
No abstract availableThis publication has 23 references indexed in Scilit:
- Stoichiometry of covalent actin-subfragment 1 complexes formed on reaction with a zero-length crosslinking compoundBiochemistry, 1984
- Mapping of actin-binding sites on the heavy chain of myosin subfragment 1Biochemistry, 1983
- Effects of tryptic digestion on myosin subfragment- 1 and its actin-activated ATPaseBiochemistry, 1982
- Structure of the actin–myosin interfaceNature, 1981
- Proteolytic approach to structure and function of actin recognition site in myosin headsBiochemistry, 1981
- The limited tryptic cleavage of chymotryptic S-1 : An approach to the characterization of the actin site in myosin headsBiochemical and Biophysical Research Communications, 1979
- Location of SH-1 and SH-2 in the heavy chain segment of heavy meromyosinArchives of Biochemistry and Biophysics, 1978
- Cyanogen bromide peptide from bovine cardiac myosin containing two essential thiols Evidence for sequence homology with skeletal myosin in the region of the active siteFEBS Letters, 1977
- Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulfateAnalytical Biochemistry, 1971
- [94] Myosin adenosinetriphosphatasePublished by Elsevier ,1955