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从猪心肌中提取的原肌球蛋白(TM),用2,2,6,6-四甲基-4-(二氯三氮嗪代)氨基哌啶-1-氧基进行自旋标记。产物(SL-TM)的ESR波谱属弱固定型。观察了三种变性手段(热、盐酸胍、脲)对上述波谱的影响。SL-TM经酶解后所得ESR波谱与标记物稀溶液的波谱相似,由此测定SL-TM中标记物的结合量。对SL-TM进行变温测定所得Arrhenius图显示两个转折点(TM的构象转变温度),约为45℃和74—75℃,后一种温度迄今未见文献报道。而SL-TM的酶降解产物在对微波功率饱和与变温的响应中的行为则与之截然不同。
Myosin (TM) extracted from porcine myocardium was spin-labeled with 2,2,6,6-tetramethyl-4- (dichlorotriazinyl) aminopiperidine-1-oxyl. The ESR spectrum of the product (SL-TM) is weakly fixed. The effects of three denaturation methods (heat, guanidine hydrochloride, urea) on these spectra were observed. The ESR spectrum of SL-TM after enzymatic hydrolysis was similar to that of the dilute solution of labeled product, and the amount of bound label in SL-TM was determined. The Arrhenius plot of temperature-dependent SL-TM measurements shows two turning points (the conformational transition temperature of TM) of about 45 ° C and 74-75 ° C. The latter temperature has not hitherto been reported. The behavior of SL-TM enzyme degradation products in response to microwave power saturation and temperature changes is quite different.