Interaction of Paratropomyosin with β-Connectin and Its 400-kiloDalton Fragment from Chicken Skeletal Muscle as Influenced by the Calcium Ion Concentration

1999 ◽  
Vol 63 (8) ◽  
pp. 1425-1432 ◽  
Author(s):  
Sha FEI ◽  
Minoru YAMANOUE ◽  
Takahide OKAYAMA
Keyword(s):  
Skeletal Muscle ◽  
Calcium Ion ◽  
Ion Concentration ◽  
Calcium Ion Concentration ◽  
Chicken Skeletal Muscle

scholarly journals ADENOSINE TRIPHOSPHATE-LINKED CONCENTRATION OF CALCIUM IONS IN A PARTICULATE FRACTION OF RABBIT MUSCLE

1962 ◽  
Vol 14 (3) ◽  
pp. 389-400 ◽  
Author(s):  
Setsuro Ebashi ◽  
Fritz Lipmann
Keyword(s):  
Skeletal Muscle ◽  
Endoplasmic Reticulum ◽  
Electron Micrographs ◽  
Calcium Ions ◽  
Calcium Ion ◽  
Membrane Fraction ◽  
Ion Concentration ◽  
Rabbit Muscle ◽  
Differential Centrifugation ◽  
Calcium Ion Concentration

ATPase and ATP-dependent calcium ion concentration was studied with a membrane fraction isolated from homogenized rabbit skeletal muscle by differential centrifugation. Electron micrographs of the fraction indicate that it consists mainly of resealed tubules and vesicles of the endoplasmic reticulum. The up-to-1400-fold concentration of calcium in this fraction might be explained by proposing the existence of an energy-requiring system for the transport of calcium ions into the tubules or vesicles.

scholarly journals Fluorescence microscope study of the binding of added C protein to skeletal muscle myofibrils.

1981 ◽  
Vol 90 (1) ◽  
pp. 25-31 ◽  
Author(s):  
C Moos
Keyword(s):  
Skeletal Muscle ◽  
Fluorescence Microscopy ◽  
Calcium Ion ◽  
Ion Concentration ◽  
Free Calcium ◽  
Myofibrillar Atpase ◽  
C Protein ◽  
Thick Filaments ◽  
Calcium Ion Concentration

The binding of extra C protein to rabbit skeletal muscle myofibrils has been investigated by fluorescence microscopy with fluorescein-labeled C protein or unmodified C protein plus fluorescein-labeled anti-C protein. Added C protein binds strongly to the I bands, which is consistent with its binding to F actin in solution (Moos, C., C. M. Mason, J. M. Besterman, I. M. Feng, and J. H. Dubin. 1978. J. Mol. Biol. 124:571-586). Of particular interest, the binding to the I band is calcium regulated: it requires a free calcium ion concentration comparable to that which activates the myofibrillar ATPase. This increases the likelihood that C protein-actin interaction might be physiologically significant. When I band binding is suppressed, binding in the A band becomes evident. It appears to occur particularly near the M line, and possibly at the edges of the A band as well, suggesting that those parts of the thick filaments that lack C protein in vivo may nevertheless be capable of binding added C protein.

Model of short-term regulation of calcium-ion concentration

SIMULATION ◽  
1979 ◽  
Vol 32 (6) ◽  
pp. 193-204 ◽  
Author(s):  
George G. Járos ◽  
Thomas G. Coleman ◽  
Arthur C. Guyton
Keyword(s):  
Calcium Ion ◽  
Ion Concentration ◽  
Short Term ◽  
Calcium Ion Concentration

Bile canalicular contraction in the isolated hepatocyte doublet is related to an increase in cytosolic free calcium ion concentration

2008 ◽  
Vol 8 (3) ◽  
pp. 178-183 ◽  
Author(s):  
Sumio Watanabe ◽  
Masahiro Tomono ◽  
Makoto Takeuchi ◽  
Tsuneo Kitamura ◽  
Miyoko Hirose ◽  
...  
Keyword(s):  
Calcium Ion ◽  
Ion Concentration ◽  
Free Calcium ◽  
Cytosolic Free Calcium ◽  
Bile Canalicular Contraction ◽  
Calcium Ion Concentration
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