Heterogeneity in Enzymatic Sites of Heavy Meromyosin Shown by Measuring F-Actin-Inactivated Hydrolysis of β-Naphthyl Triphosphate1
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/92/5/1577/2687136/92-5-1577.pdf
Cited by 4 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. Characterization of the ATPase Active Site in Myosin Subfragment-1 with the Use of Vanadate plus ADP as a Reversible “Affinity-Labeling” Reagent: Evidence for Heterogeneity in the Active Sites1;The Journal of Biochemistry;1985-09
2. Relationship between the ATPase Activity and the ATP-Induced Fluorescence Enhancement of SH-Modified Heavy Meromyosin during Its Fractional Inactivation by Vanadate plus ADP: Evidence for Heterogeneity in the Active Sites1;The Journal of Biochemistry;1985-06
3. Structural difference between two ATP-binding sites of heavy meromyosin revealed by the dynamic fluorescence quenching technique;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1984-06
4. Transient kinetics of the binding of ATP to actomyosin subfragment 1: evidence that the dissociation of actomyosin subfragment 1 by ATP leads to a new conformation of subfragment 1;Biochemistry;1984-05-22
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