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2'(或3')-O-(2,4,6-三硝基苯基)腺苷5'-三磷酸的荧光特性及其在与重酶解肌球蛋白ATP酶结合研究中的应用。

Fluorescence properties of 2' (or 3')-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate and its use in the study of binding to heavy meromyosin ATPase.

作者信息

Hiratsuka T

出版信息

Biochim Biophys Acta. 1976 Nov 26;453(1):293-7. doi: 10.1016/0005-2795(76)90277-4.

Abstract

2' (or 3')-O-(2,4,6-Trinitrophenyl) adenosine 5'-triphosphate (N3ph-ATP), which contains a Meisenheimer complex moiety, is one of the class of compounds which do not fluoresce in water but fluoresce both in low polarity solvents and when bound to the protein molecule. Fluorescence intensity of N3ph-ATP in the range of 540 nm, when excited at 410 nm, decreased with increasing the solvent polarity accompanying the increment of the wavelength of maximum emission. When bound to heavy meromyosin ATPase, the fluorescence properties of N3ph-ADP were almost the same as those of N3ph-ATP in a low polarity solvent, suggesting that N3ph-ADP was bound to hydrophobic area on heavy meromyosin ATPase.

摘要

2'(或3')-O-(2,4,6-三硝基苯基)腺苷5'-三磷酸(N3ph-ATP)含有迈森海默络合物部分,是一类在水中不发荧光,但在低极性溶剂中以及与蛋白质分子结合时都会发荧光的化合物之一。当在410nm激发时,N3ph-ATP在540nm范围内的荧光强度随着溶剂极性的增加以及最大发射波长的增加而降低。当与重酶解肌球蛋白ATP酶结合时,N3ph-ADP的荧光特性与在低极性溶剂中的N3ph-ATP几乎相同,这表明N3ph-ADP与重酶解肌球蛋白ATP酶上的疏水区域结合。

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