Evidence from oxygen exchange studies that the two heads of myosin are functionally different.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference33 articles.
1. Mechanism of adenosine triphosphate hydrolysis by actomyosin
2. The characterization of myosin–product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reaction
3. Mechanism of the actomyosin ATPase: effect of actin on the ATP hydrolysis step.
4. Distribution of [18O]Pi species from [gamma-18O]ATP hydrolysis by myosin and heavy meromyosin. Evidence for two kinds of myosin-active site differing in their rate of intermediate oxygen exchange.
Cited by 8 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. Deoxyadenosine triphosphate acting as an energy-transferring molecule in adenosine deaminase inhibited human erythrocytes;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1991-09
2. Kinetics of ATP and inorganic phosphate release during hydrolysis of ATP by rabbit skeletal actomyosin subfragment 1. Oxygen exchange between water and ATP or phosphate.;Journal of Biological Chemistry;1990-01
3. Measurement of the reversibility of ATP binding to myosin in calcium-activated skinned fibers from rabbit skeletal muscle;Journal of Biological Chemistry;1989-05
4. Two pathways for oxygen exchange by heavy meromyosin and their dependence on actin.;Journal of Biological Chemistry;1988-04
5. Active-site titration of enzymes at high concentration. Application to myosin ATPase;European Journal of Biochemistry;1986-12
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