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- W2007863335 abstract "It was found that the fluorescence of 1,N6-ethenoadenosine triphosphate (ε-ATP) bound to myosin subfragment-1 (S-1) is resistant to quenching by acrylamide, while free ε-ATP is effectively quenched. Thus in the presence of acrylamide the bound ε-ATP is still highly fluorescent, while free ε-ATP is much less fluorescent. The Stern-Volmer constants of bound and free ε-ATP are 6.83 and 57.86 M−1, respectively. Therefore it is easy to distinguish spectro-scopically the nucleotide-ligated S-1 from nucleotide-free S-1. Moreover acrylamide does not alter the S-1-Mg2+-ε-ATPase behavior." @default.
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- W2007863335 date "1982-11-01" @default.
- W2007863335 modified "2023-10-14" @default.
- W2007863335 title "Spectroscopic isolation of ES complexes of myosin subfragment-1 ATPase by fluorescence quenching" @default.
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- W2007863335 doi "https://doi.org/10.1016/0006-291x(82)91557-1" @default.
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