Sequence determination of a peptide fragment from electric eel acetylcholinesterase, involved in the binding of quaternary ammonium

FEBS Letters

Hirth, Christian¹  Chang, Jui-Yoa²  Goeldner, Maurice¹  Kieffer, Brigitte¹  Aebersold, Ruedi² 

[1] Laboratoire de Chimie Bio-organique, UA 31 CNRS, Faculté de Pharmacie, 74, route du Rhin, BP 10, 67048 Strasbourg Cedex, France;Laboratoire de Chimie Bio-organique, UA 31 CNRS, Faculté de Pharmacie, Ciba Geigy, Basel, Switzerland

关键词: Photoaffinity labeling Aryldiazonium salt Acetylcholinesterase Quaternary ammonium binding site Peptide sequence;    AChE;    acetylcholinesterase;    DDF;    p-(N;    N-dimethylamino)benzenediazonium fluoroborate;    PTH;    phenylthiohydantoin;    PTZ;    phenylthiazolinone;    DABITC;    p-(N;    N-dimethylamino)azobenzene isothiocyanate;    DABTH;    p-(N;    N-dimethylamino)azobenzene thiohydantoin;   

DOI  :  10.1016/0014-5793(86)80655-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Specific photoaffinity labelling of purified electric eel acetylcholinesterase by ³H-labelled p-(N,N-dimethyl-amino) benzenediazonium fluoroborate allows the identification of a labelled peptide fragment which is described as being involved in the binding of quaternary ammonium ions on this enzyme. Denaturation and proteolytic cleavage of the inactivated enzyme gave a mixture of peptide fragments. The purification of one labelled fragment, containing over 15% of the radioactivity incorporated in the enzyme, led to the following sequence: Gly-Ser-X-Phe. The relatively low amount of this tetrapeptide did not allow us to determine the nature of the labelled residue X.

【 授权许可】

Unknown