Derivative spectroscopy of tryptophan fluorescence used to study conformational transitions in the (Ca2+ + Mg2+)-adenosine triphosphatase of sarcoplasmic reticulum

1986 ◽  
Vol 874 (3) ◽  
pp. 305-311 ◽  
Author(s):  
Colin J. Restall ◽  
Mark Coke ◽  
Elizabeth Phillips ◽  
Dennis Chapman
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Adenosine Triphosphatase ◽  
Tryptophan Fluorescence ◽  
Conformational Transitions ◽  
Derivative Spectroscopy

scholarly journals Characterization of the tryptophan fluorescence from sarcoplasmic reticulum adenosine triphosphatase by frequency-domain fluorescence spectroscopy

Biochemistry ◽  
1989 ◽  
Vol 28 (8) ◽  
pp. 3490-3498 ◽  
Author(s):  
Ignacy Gryczynski ◽  
Wieslaw Wiczk ◽  
Giuseppe Inesi ◽  
Thomas Squier ◽  
Joseph R. Lakowicz
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Fluorescence Spectroscopy ◽  
Frequency Domain ◽  
Adenosine Triphosphatase ◽  
Tryptophan Fluorescence

The Influence of Detergents on the Ca2+-and Mg2+-Dependent Adenosine Triphosphatase of the Sarcoplasmic Reticulum

1982 ◽  
Vol 37 (3-4) ◽  
pp. 299-307 ◽  
Author(s):  
Hans Lüdi ◽  
Bernhard Rauch ◽  
Wilhelm Hasselbach
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Ions ◽  
Inorganic Phosphate ◽  
Adenosine Triphosphatase ◽  
Tryptophan Fluorescence ◽  
The Other ◽  
Phosphorylated Protein ◽  
Intrinsic Tryptophan Fluorescence ◽  
Low Concentrations ◽  
Calcium Affinity

Abstract During the stepwise solubilization of sarcoplasmic reticulum vesicles with detergents, the following changes in the structural and enzymatic properties of the preparation are observed: 1. The viscosity of the vesicular suspension initially rises. This change is accompanied by the formation of elongated tubules. Subsequently the membranes are completely desintegrated, resulting in a considerable reduction of the viscosity. 2. A decrease in the activity of the Ca2+-dependent ATPase, which is restored after complete solubilization. 3. A decrease in the change of intrinsic tryptophan-fluorescence on removal of calcium ions, which is also restored after complete solubilization. 4. A decrease of the calcium affinity of the ATPase. 5. A decrease in the amount of phosphorylated protein formed by the incorporation of inorganic phosphate. On the other hand, the amount of phosphoprotein formed from ATP is not affected during solubilization. 6. The dependence of the initial rates of phosphoprotein formation from inorganic phosphate on either magnesium or inorganic phosphate at low concentrations of the respective ligand changes from an S-shape profile to a normal hyperbolic profile after solubilization.

Stimulation of adenosine triphosphatase activity of sarcoplasmic reticulum by adenylyl methylene diphosphate

1978 ◽  
Vol 526 (2) ◽  
pp. 591-596 ◽  
Author(s):  
Munekazu Shigekawa ◽  
Alfred A. Akowitz ◽  
Arnold M. Katz
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Adenosine Triphosphatase ◽  
Adenosine Triphosphatase Activity ◽  
Stimulation Of
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