Structural studies of rigor bovine myofibrils using fluorescence microscopy. II. Influence of sarcomere length on the binding of myosin subfragment-1, alpha-actinin and G-actin to rigor myofibrils
- 31 December 1993
- journal article
- Published by Elsevier BV in Meat Science
- Vol. 33 (2), 157-190
- https://doi.org/10.1016/0309-1740(93)90058-p
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- A study of the histological changes in the growing muscles of beef animalsInternational Journal of Food Science & Technology, 2007
- Factors influencing the ascending limb of the sarcomere length‐tension relationship in rabbit skinned muscle fibres.The Journal of Physiology, 1987
- Binding of heavy meromyosin and subfragment-1 to thin filaments in myofibrils and single muscle fibersBiochemistry, 1980
- All myosin heads form bonds with actin in rigor rabbit skeletal muscleBiochemistry, 1980
- Structural changes in beef muscle during ageingJournal of the Science of Food and Agriculture, 1976
- EFFECTS OF PRE‐RIGOR TENSION ON TENDERNESS OF INTACT BOVINE AND OVINE MUSCLEJournal of Food Science, 1974
- A COMPARISON OF THE EFFECTS OF AGING, CONDITIONING AND SKELETAL RESTRAINT ON THE TENDERNESS OF MUTTONJournal of Food Science, 1973
- Control of muscle contractionQuarterly Reviews of Biophysics, 1969
- Shortening as a factor in meat ageingInternational Journal of Food Science & Technology, 1967
- THE USE OF FLUORESCEIN-LABELED HEAVY MEROMYOSIN FOR THE CYTOLOGICAL DEMONSTRATION OF ACTINThe Journal of cell biology, 1965