Rabbit skeletal muscle F-actin can be stable at low ionic strength, provided trace amounts of Ca2+ are absent
- 1 April 1979
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 577 (2) , 267-272
- https://doi.org/10.1016/0005-2795(79)90030-8
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Dual effect of Ca2+ on ultrasonic ATPase activity and polymerization of muscle actinBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- Actin polymerization and interaction with other proteins in temperature-induced gelation of sea urchin egg extracts.The Journal of cell biology, 1976
- Transformation of cytoplasmic actin importance for the organization of the contractile gel reticulnm and the contraction ? relaxation cycle of cytoplasmic actomyosinCell and tissue research, 1976
- The mechanochemical basis of amoeboid movementExperimental Cell Research, 1976
- Interactions of actin, myosin, and a new actin-binding protein of rabbit pulmonary macrophages. II. Role in cytoplasmic movement and phagocytosis.The Journal of cell biology, 1976
- The role of actin in the temperature-dependent gelation and contraction of extracts of Acanthamoeba.The Journal of cell biology, 1976
- Effect of calcium ions on the flexibility of reconstituted thin filaments of muscle studied by quasielastic scattering of laser lightJournal of Molecular Biology, 1972
- Regulation in molluscan musclesJournal of Molecular Biology, 1970
- Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscleJournal of Molecular Biology, 1963
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951