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- W2016066638 abstract "Abstract The graphs showing the relationships between the logarithms of the fluorescence intensities of ATPase (EC 3.6.1.3) from Bacillus stearothermophilus and of 8-anilino-1-naphthalenesulfonic acid bound to the enzyme and the reciprocal of temperature both exhibit sharp breaks at 50°C. Similar relationships are observed in the presence of ATP (ADP) and Mg 2+ . The results suggest that a thermal transition in the conformation of the enzyme may occur at 50°C, both in the absence and presence of ATP(ADP) and Mg 2+ ." @default.
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- W2016066638 date "1973-08-01" @default.
- W2016066638 modified "2023-09-27" @default.
- W2016066638 title "Conformational change with temperature of ATPase from Bacillus stearo-thermophilus" @default.
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- W2016066638 doi "https://doi.org/10.1016/0005-2744(73)90281-7" @default.
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