Abstract
When myosin subfragment 1 derivatives in which the reactive sulfhydryl SH1 has been blocked react with N,N'-p-phenylenedimaleimide or 5,5'-dithiobis(2-nitrobenzoic acid), the reactive sulfhydryl group SH2 of the 20-kDa domain is crosslinked with a thiol of the 50-kDa domain of the heavy chain. The crosslink induces the stable trapping of a significant amount of Mg2+-nucleotide in the ATPase site.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenine Nucleotides / metabolism*
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Adenosine Triphosphatases / antagonists & inhibitors
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Adenosine Triphosphatases / metabolism*
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Animals
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Binding Sites
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Calcium-Transporting ATPases / metabolism
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In Vitro Techniques
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Kinetics
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Macromolecular Substances
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Magnesium / metabolism
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Myosin Subfragments
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Myosins / metabolism*
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Peptide Fragments / metabolism*
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Rabbits
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Sulfhydryl Compounds
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Sulfhydryl Reagents / pharmacology
Substances
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Adenine Nucleotides
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Macromolecular Substances
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Myosin Subfragments
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Peptide Fragments
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Sulfhydryl Compounds
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Sulfhydryl Reagents
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Adenosine Triphosphatases
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Myosins
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Calcium-Transporting ATPases
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Magnesium