Carlson B J, Raftery M A
Department of Biochemistry, University of Minnesota, St. Paul 55108.
Biochemistry. 1993 Jul 27;32(29):7329-33. doi: 10.1021/bi00080a002.
The beta- and delta-subunits of the nicotinic acetylcholine receptor from Torpedo californica were covalently photolabeled at the synaptic surface with the ATP photoaffinity analogue [alpha-32P]-8-azido-ATP. The specificity of labeling for nucleotide binding sites was demonstrated by the saturation of labeling with increasing concentration of 8-azido-ATP and the inhibition of photolabeling by ATP. Protection studies suggest that the binding sites for the photolabel are unique and are not associated with the cholinergic ligand binding sites.
用ATP光亲和类似物[α-32P]-8-叠氮基ATP对来自加州电鳐的烟碱型乙酰胆碱受体的β亚基和δ亚基在突触表面进行共价光标记。通过增加8-叠氮基ATP浓度使标记饱和以及ATP对光标记的抑制，证明了对核苷酸结合位点标记的特异性。保护研究表明，光标记的结合位点是独特的，且与胆碱能配体结合位点无关。
