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
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/97/6/1583/2713656/97-6-1583.pdf
Cited by 5 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. Interaction of vanadate with uridine and adenosine monophosphate. Formation of ADP and ATP analogs;Journal of the American Chemical Society;1988-08
2. Separation of SH-Modified Myosin Subfragment-1(A1) Isozyme into Two Distinct Equimolar Fractions by an Affinity Chromatography1;The Journal of Biochemistry;1988-01
3. Active-site titration of enzymes at high concentration. Application to myosin ATPase;European Journal of Biochemistry;1986-12
4. Vanadium(V) oxyanions: the interaction of vanadate with pyrophosphate, phosphate, and arsenate;Journal of the American Chemical Society;1986-10
5. 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
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