Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility
- 1 April 1977
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 111 (2) , 129-157
- https://doi.org/10.1016/s0022-2836(77)80119-8
Abstract
No abstract availableThis publication has 42 references indexed in Scilit:
- Light Chains from Slow‐Twitch Muscle Myosin.European Journal of Biochemistry, 1976
- Separation of two HMM-S1 species from white muscle myosinBiochemical and Biophysical Research Communications, 1976
- Myosin from cross‐reinnervated cat muscles. Evidence for reciprocal transformation of heavy chainsFEBS Letters, 1975
- X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscleJournal of Molecular Biology, 1975
- Evidence for structural changes in vertebrate thick filaments induced by calciumJournal of Molecular Biology, 1974
- Role of myosin light chains in calcium regulationNature, 1974
- Meterogeneity of subfragment-1 preparations from myofibril digestion by trypsinBiochemical and Biophysical Research Communications, 1973
- Substructure of the myosin molecule: IV. Interactions of myosin and its subfragments with adenosine triphosphate and F-actinJournal of Molecular Biology, 1973
- Substructure of the myosin moleculeJournal of Molecular Biology, 1971
- The electrophoretic homogeneity of the myosin subunitsBiochimica et Biophysica Acta, 1961