与三磷酸腺苷（ATP）和5'-[γ-硫代]三磷酸腺苷（adenosine 5'-[γ-thio]triphosphate）结合到骨骼肌肌球蛋白亚片段1和肌动球蛋白亚片段1相关的蛋白质荧光变化。

Protein fluorescence changes associated with ATP and adenosine 5'-[gamma-thio]triphosphate binding to skeletal muscle myosin subfragment 1 and actomyosin subfragment 1.

Millar N C, Geeves M A

Department of Biochemistry, University of Bristol, U.K.

Biochem J. 1988 Feb 1;249(3):735-43. doi: 10.1042/bj2490735.

Abstract

The fluorescence changes accompanying the binding of ATP and adenosine 5'-[gamma-thio]triphosphate (ATP gamma S) to myosin subfragment 1 (S1) and actomyosin subfragment 1 (actoS1) have been reinvestigated at 20 degrees C and 1 degree C, pH 7.0, 0.1 M-KCl. 2. Two successive fluorescence enhancements are observed following ATP binding to both S1 and actoS1. 3. The slow fluorescence change has the same rate with S1 and actoS1, and is due to the ATP cleavage step. 4. With actoS1 the fast fluorescence change occurs after dissociation, so a new intermediate, S1 ATP, is required on the actoS1 pathway. 5. The dissociation of actoS1 by ATP gamma S results in a fluorescence enhancement with the same apparent rate as dissociation, but indirect evidence suggests that this too occurs on a dissociated state.

摘要

在20℃和1℃、pH 7.0、0.1M - KCl条件下，对ATP和腺苷5'-[γ-硫代]三磷酸（ATPγS）与肌球蛋白亚片段1（S1）和肌动球蛋白亚片段1（肌动蛋白S1）结合时伴随的荧光变化进行了重新研究。2. ATP与S1和肌动蛋白S1结合后均观察到两个连续的荧光增强。3. 缓慢的荧光变化在S1和肌动蛋白S1上具有相同的速率，并且是由于ATP裂解步骤。4. 对于肌动蛋白S1，快速荧光变化发生在解离之后，因此在肌动蛋白S1途径上需要一个新的中间体S1 ATP。5. ATPγS使肌动蛋白S1解离导致荧光增强，其表观速率与解离相同，但间接证据表明这也发生在解离状态。