α‐Toxin binding to acetylcholine receptor α179–191 peptides: Intrinsic fluorescence studies

FEBS Letters

Levinson, L.S.¹  Low, B.W.²  Radding, W.²  Hashim, G.A.³  Corfield, P.W.R.² 

[1] Protein Chemistry Core Facility, Howard Hughes Institute, New York, NY 10032, USA;Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th Street, New York, NY 10032, USA;Department of Microbiology-Surgery, Columbia University, 630 West 168th Street, New York, NY 10032, USA

关键词: Acetylcholine receptor α-subunit;    α-Toxin binding region;    α-Cobratoxin;    Erabutoxin a;    Synthetic peptide;    Intrinsic fluorescence;    AChR;    acetylcholine receptor;    ACh;    acetylcholine;    α-CbTX;    α-cobratoxin;    Ea;    erabutoxin a;    HPLC;    high-performance liquid chromatography;    PBS;    phosphate-buffered saline;    FPLC;    fast performance liquid chromatography;   

DOI  :  10.1016/0014-5793(88)80733-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Interactions between two α-toxins and the synthetic peptides α179–191 from both calf and human acetylcholine receptor α-subunit sequences have been studied by measurements of quenching of intrinsic fluorescence after toxin addition. Dissociation constants of approx. 5 × 10⁻⁸ M for binding of calf peptide by both α-cobratoxin and erabutoxin a have been estimated. The binding of α-cobratoxin to calf peptide, which leads to marked quenching of fluorescence intensity, is inhibited by a 10⁴ molar excess of acetylcholine. The human α179–191 peptide binds to α-cobratoxin, but not, under comparable conditions, to erabutoxin a.

【 授权许可】

Unknown