Binding properties of a locust's chemosensory protein
Binding properties of a locust's chemosensory protein
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DOI：
10.1016/s0006-291x(02)00185-7
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发表时间：
2002-04-26
影响因子：
3.1
通讯作者：
Pelosi, P
中科院分区：
文献类型：
--
作者：
Ban, LP;Zhang, L;Pelosi, P
在荧光结合实验中，沙漠蝗虫（Schistocerca gregaria）的化学感受蛋白CSP - sg4可逆地结合N - 苯基 - 1 - 萘胺，其解离常数为4μM。当与该蛋白结合时，荧光探针的发射峰发生明显的蓝移，同时最大强度增加一个数量级。该实验还能够测量CSP对其他芳香族和脂肪族化合物的亲和力。这种蛋白的结合能力在100℃热处理20分钟的情况下不受影响。化学感受蛋白的配体结合特性可能有助于阐明这一最近发现的可溶性蛋白类别在化学感受中的作用。（C）2002爱思唯尔科学（美国）。保留所有权利。
The chemosensory protein CSP-sg4 of the desert locust Schistocerca gregaria binds reversibly N-phenyl-1-naphthylamine in fluorescent-binding assays. with a dissociation constant of 4 muM. Upon binding to the protein, the emission peaks of the fluorescent probe undergo a marked blue shift, accompanied by an order of magnitude increase of the maximum intensity. The assay has also allowed the measurement of the affinity of CSP to other aromatic and aliphatic compounds. The binding capacity of this protein is unaffected by thermal treatments tip to 100 degreesC for 20 min. The ligand-binding characteristics of chemosensory proteins may help in clarifying the role of this recently discovered class of soluble proteins in chemoreception. (C) 2002 Elsevier Science (USA). All rights reserved.