Activity and conformational changes of α‐chymotrypsin in reverse micelles studied by spin labeling

FEBS Letters

Pinzino, C.¹  Marzola, P.²  Forte, C.¹  Veracini, C.A.² 

[1] Instituto di Chimica Quantistica ed Energetica Molecolare, via Risorgimento 35, 56126 Pisa, Italy;Dipartimento di Chimica e Chimica Industriale, via Risorgimento 35, 56126 Pisa, Italy

关键词: α-Chymotrypsin;    AOT;    ESR;    Reserve micelle;    Spin labeling;   

DOI  :  10.1016/0014-5793(91)80901-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

α-Chymotrypsin (CT), spin-labeled at the active site by using an acylating label which constitutes a substrate for this protein, has been investigated in reverse micelles formed by AOT in isooctane. The electron spin resonance spectra provided information on conformation, dynamics and deacylation activity. The dynamics of the label bound to CT appears to be more hindered in reverse micelles than in aqueous solution, probably owing to the effect of the micellar environment on protein conformation. The deacylation rate in reverse micelles does not show the characteristic bell-shaped dependence on water content which is generally found for CT enzymatic activity.

【 授权许可】

Unknown