Binding properties of a locust's chemosensory protein

被引：102

作者：

Ban, LP

Zhang, L

Yan, YH

Pelosi, P

机构：

[1] Univ Pisa, Dipartimento Chim & Biotecnol Agr, I-26124 Pisa, Italy

[2] China Agr Univ, Dept Entomol, Beijing, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2002年 / 293卷 / 01期

关键词：

chemosensory proteins; pheromone; chemical communication; fluorescence-binding assay; N-phenylnaphthylamine; Schistocerca gregoria;

D O I：

10.1016/S0006-291X(02)00185-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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页码：50 / 54

页数：5

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