scholarly journals Crossbridge-mediated Activation of Rabbit Skeletal Muscle Myofibrillar ATPase: a Role for the Calcium Binding Domains of Troponin C

2009 ◽  
Vol 96 (3) ◽  
pp. 226a
Author(s):  
Franklin Fuchs ◽  
Zenon Grabarek
Keyword(s):  
Skeletal Muscle ◽  
Calcium Binding ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
Myofibrillar Atpase ◽  
Binding Domains

scholarly journals Utilization of troponin C as a model calcium-binding protein for mapping of the calmodulin-binding sites of caldesmon

1997 ◽  
Vol 321 (3) ◽  
pp. 873-878 ◽  
Author(s):  
Alexei A. POLYAKOV ◽  
Nikolai B. GUSEV
Keyword(s):  
Skeletal Muscle ◽  
Atpase Activity ◽  
Binding Sites ◽  
Calcium Binding ◽  
Binding Protein ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
Actomyosin Atpase ◽  
Calmodulin Binding ◽  
Central Helix

Troponin C, a structural analogue of calmodulin, was used for mapping the calmodulin-binding sites of caldesmon. The apparent Kd values for the formation of the caldesmonŐcalcium-binding-protein complex as determined by native gel electrophoresis were 0.5, 1.2 and 3.9 ƁM for calmodulin, rabbit skeletal muscle troponin C and bovine cardiac troponin C respectively. Troponin C induced a 4Ő6 nm blue shift of the Trp fluorescence of caldesmon without affecting the amplitude of fluorescence. In the presence of Ca2+, troponin C induced partial displacement of caldesmon from actinŐtropomyosin complexes. Addition of 5,5ƀ-dithiobis(nitrobenzoic) acid to an equimolar complex of caldesmon and troponin C induced disulphide cross-linking between Cys-98 of rabbit skeletal muscle troponin C and the single Cys residue of duck gizzard caldesmon, located in a position analogous to Cys-580 of the chicken gizzard protein. The cross-linked caldesmonŐtroponin C complex was ineffective in inhibiting actomyosin ATPase activity. It is concluded that Cys-580 of caldesmon can be located close to both the central helix of calcium-binding proteins and the C-terminal domain of actin. This may be important for the regulation of actomyosin ATPase activity by caldesmon.

Disparate contributions of Tyr10and Tyr109to fluorescence intensity of rabbit skeletal muscle troponin C identified using a genetically engineered mutant

FEBS Letters ◽  
1994 ◽  
Vol 354 (2) ◽  
pp. 135-139 ◽  
Author(s):  
David Keleti ◽  
Venu G. Rao ◽  
Hong Su ◽  
Arvind B. Akella ◽  
Xiao-Ling Ding ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Fluorescence Intensity ◽  
Troponin C ◽  
Genetically Engineered ◽  
Rabbit Skeletal Muscle
Sign in / Sign up

Export Citation Format

Share Document