Rooney R D, Maffe W, Niemann J C, Petersen N S
Department of Molecular Biology, University of Wyoming, Laramie 82071.
Biochim Biophys Acta. 1990 Apr 23;1034(1):102-6. doi: 10.1016/0304-4165(90)90159-t.
The ATP photoaffinity analogue 8-azidoadenosine 5'-triphosphate (8N3ATP) was used to identify changes which occur in ATP binding proteins in Drosophila salivary glands following heat shock. Photolabeling experiments were done on salivary gland homogenates. Photoincorporation of 8N3ATP was observed in several proteins in both 25 degrees C control and 35 degrees C heat-shocked samples. A 42 kDa protein showed a decrease in the level of photoincorporation observed at saturation with the analogue following heat shock. A 2 min heat shock is enough to induce the effect. Protection against photolabeling was observed with low concentrations (5 microM) of ATP, while excess GTP did not protect, demonstrating that the nucleotide binding site is specific for ATP. The change is rapid enough to suggest that it is one of the earliest cellular changes in response to heat shock.
ATP光亲和类似物8-叠氮腺苷5'-三磷酸（8N3ATP）被用于鉴定果蝇唾液腺热休克后ATP结合蛋白中发生的变化。对唾液腺匀浆进行了光标记实验。在25℃对照和35℃热休克样品的几种蛋白质中均观察到8N3ATP的光掺入。一种42 kDa的蛋白质在热休克后与类似物饱和时观察到的光掺入水平降低。2分钟的热休克足以诱导这种效应。在低浓度（5 microM）的ATP存在下观察到对光标记的保护作用，而过量的GTP则没有保护作用，这表明核苷酸结合位点对ATP具有特异性。这种变化足够迅速，表明它是对热休克最早的细胞变化之一。
