The binding of myosin subfragment 1 to actin can be measured by proteolytic rates method.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference22 articles.
1. Tryptic cleavage and substructure of bovine cardiac myosin subfragment 1
2. Actin-attached and detached crossbridges in myofibrils: Segregation into two populations according to their sensitivity to proteolytic digestion of myosin heavy chain
3. Kinetic rates of tryptic digestion of bovine cardiac myofibrils. An improved measurement of cross-bridge dissociation.
4. Location of SH-1 and SH-2 in the heavy chain segment of heavy meromyosin
5. Effect of bridging the two essential thiols of myosin on its spectral and actin-binding properties
Cited by 7 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Rigor cross-bridges bind to two actin monomers inthin filaments of rabbit psoas muscle;Journal of Molecular Biology;1995-01
2. Orientation and Dynamics of Myosin Heads in Aluminum Fluoride Induced Pre-Power Stroke States: An EPR Study;Biochemistry;1994-10-04
3. Effect of actin on the tryptic digestion of myosin subfragment 1 in the weakly attached state;European Journal of Biochemistry;1992-12
4. Effect of nucleotides, actin and temperature on thermolysin digestion of myosin subfragment-1;European Journal of Biochemistry;1990-09
5. Nucleotide-induced states of myosin subfragment 1 cross-linked to actin;Biochemistry;1989-04-18
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