June 21, 1983Biochemistry
Tropomyosin-troponin and tropomyosin-actin interactions: a fluorescence quenching study
Key result
The presence of troponin or F-actin interacting with tropomyosin near the Cys-190 site induced a second, longer-lived fluorescence decay component and decreased the quenching rate constant.
Population
Rabbit skeletal alpha alpha-tropomyosin labeled at Cys-190 with the fluorescent probe 1,5-IAE-DANS
Comparison
Addition of troponin or F-actin vs Tropomyosin alone
Design
Preclinical
Authors
Discussion
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Member takes
Implication
Refines thin filament models in cardiac muscle; extends biochemical data but leaves functional impact in vivo open.
Structured PICO
P
Population
Rabbit skeletal alpha alpha-tropomyosin labeled at Cys-190 with the fluorescent probe 1,5-IAE-DANS
I
Intervention
Addition of troponin or F-actin
C
Comparator
Tropomyosin alone
O
Outcome
Fluorescence decay lifetime and quenching constants (Ksv' and kq)surrogate
Fluorescence quenching studies demonstrate that troponin and actin interact with tropomyosin near the Cys-190 site, altering the local environment from hydrophilic to hydrophobic.
Cite This Study
Lamkin et al. (1983) studied this question. Troponin and F-actin vs. Tropomyosin alone was evaluated on Fluorescence decay and quenching constants. The presence of troponin or F-actin interacting with tropomyosin near the Cys-190 site induced a second, longer-lived fluorescence decay component and decreased the quenching rate constant.