Thiolysis of dinitrophenylated sulfhydryl groups in gizzard myosin. Restoration of regulatory properties in a reconstituted actomyosin.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference50 articles.
1. Dinitrophenylation of chicken gizzard myosin. Reactivity of the 17 000-dalton light chain
2. The Biochemistry of Smooth Muscle;Sobieszek,1977
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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. Reaction of thiol groups of gizzard myosin heavy chains with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole;Archives of Biochemistry and Biophysics;1990-08
2. Modification of the (Ca2 + Mg2)-ATPase protein of sarcoplasmic reticulum with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1989-04
3. Characterization of the fluorescein isothiocyanate-reactive site of gizzard myosin ATPase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1987-04
4. Trinitrophenylation of smooth muscle myosin;Biochemical and Biophysical Research Communications;1985-01
5. Modification of thiols of gizzard myosin alters ATPase activity, stability of myosin filaments, and the 6-10 S conformational transition.;Journal of Biological Chemistry;1985-01
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