摘要
Tropomyosin (TM) extracted from pig cardiac muscle was spin-labeled with 2,2,6,6-tetramethyl-4-(dichlorotriazin)-aminopiperidine-1-oxyl. The ESR spectra of the product (SL-TM) were of a type of weak immobilization. Effects of three means for the denaturation were observed on the above spectra. The ESR spectrum obtained for SL-TMafter enzymatic degradation was found to be analogous to that for the label itself in a dilute solution and thereby the quantity of labels bound in SL-TM estimated. The Arrhenius plots attained through variable temperature measurement for SL-TM’s exhibited two inflexion points (the conformational transition temperatures for TM) around 45℃ and 74-75℃, the latter temperature having not been reported in literature so far. However, the enzymatic degradation product from SL-TM behaved quite differently from it in the response to microwave power saturation and temperature variation.
Tropomyosin (TM) extracted from pig cardiac muscle was spin-labeled with 2,2,6,6-tetramethyl-4-(dichlorotriazin)-aminopiperidine-1-oxyl. The ESR spectra of the product (SL-TM) were of a type of weak immobilization. Effects of three means for the denaturation were observed on the above spectra. The ESR spectrum obtained for SL-TMafter enzymatic degradation was found to be analogous to that for the label itself in a dilute solution and thereby the quantity of labels bound in SL-TM estimated. The Arrhenius plots attained through variable temperature measurement for SL-TM's exhibited two inflexion points (the conformational transition temperatures for TM) around 45℃ and 74-75℃, the latter temperature having not been reported in literature so far. However, the enzymatic degradation product from SL-TM behaved quite differently from it in the response to microwave power saturation and temperature variation.
基金
Project supported by the National Natural Science Foundation of China
