SPECTROSCOPIC ISOLATION OF ES COMPLEXES OF MYOSIN SUBFRAGMENT-1 ATPASE BY FLUORESCENCE QUENCHING
SPECTROSCOPIC ISOLATION OF ES COMPLEXES OF MYOSIN SUBFRAGMENT-1 ATPASE BY FLUORESCENCE QUENCHING
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DOI：
10.1016/0006-291x(82)91557-1
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发表时间：
1982-01-01
影响因子：
3.1
通讯作者：
MORALES, MF
中科院分区：
文献类型：
--
作者：
ANDO, T;DUKE, JA;MORALES, MF
ε的荧光与[兔]肌球蛋白亚片段-1（S-1）结合的ATP对丙烯酰胺的淬灭有抗性，而游离的ε-ATP对丙烯酰胺的淬灭有抗性。ATP被有效地猝灭。在丙烯酰胺的存在下，结合的ε- ATP仍然是高度荧光的，而游离的ε- ATP的荧光要少得多。结合态和自由态的Stern-Volmer常数ε- ATP分别为6.83和57.86 M-1。很容易通过光谱法区分核苷酸连接的S-1和无核苷酸的S-1。芳基酰胺不改变S-1-Mg 2 +-ε- ATP酶行为
The fluorescence of .epsilon.-ATP bound to [rabbit] myosin subfragment-1 (S-1) was resistant to quenching by acrylamide, while free .epsilon.-ATP was effectively quenched. In the presence of acrylamide, the bound .epsilon.-ATP is still highly fluorescent, while free .epsilon.-ATP is much less fluorescent. The Stern-Volmer constants of bound and free .epsilon.-ATP is 6.83 and 57.86 M-1, respectively. It is easy to distinguish spectroscopically, the nucleotide-ligated S-1 from nucleotide-free S-1. Arylamide does not alter the S-1-Mg2+-.epsilon.-ATPase behavior.