Thiolysis of Dinitrophenylated Myosin with Restoration of Adenosine Triphosphatase Activity
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
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2. Reaction of Myosin with 1-Fluoro-2,4-dinitrobenzene at Low Ionic Strength
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4. Dinitrophenylation and thiolysis in the reversible labeling of a cysteine residue associated with the nicotinamide adenine dinucleotide site of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
5. Reversible dinitrophenylation of glyceraldehyde 3-phosphate dehydrogenase. Identification of the labeled site
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1. A highly sensitive fluorescent probe for detection of benzenethiols in environmental samples and living cells;Chem. Commun.;2010
2. Crystallographic findings on the internally uncoupled and near-rigor states of myosin: Further insights into the mechanics of the motor;Proceedings of the National Academy of Sciences;2002-09-24
3. Stepwise Modulation of ATPase Activity, Nucleotide Trapping, and Sliding Motility of Myosin S1 by Modification of the Thiol Region with Residues of Increasing Size;Biochemistry;2000-01-21
4. Temperature-induced changes in the flexibility of the loop between SH1 (Cys-707) and SH3 (Cys-522) in myosin subfragment 1 detected by cross-linking;Archives of Biochemistry and Biophysics;1991-10
5. Identification of the site of photocross-linking formed in the absence of magnesium nucleotide from SH2 (Cys-697) in myosin subfragment 1 labeled with 4'-maleimidylbenzophenone;Journal of Biological Chemistry;1991-02
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