AbstractIn skeletal muscles, FBPase–aldolase complex is located on α-actinin of the Z-line. In the present paper, we show evidence that stability of the complex is regulated by calcium ions. Real time interaction analysis, confocal microscopy and the protein exchange method have revealed that elevated calcium concentration decreases association constant of FBPase–aldolase and FBPase-α-actinin complex, causes fast dissociation of FBPase from the Z-line and slow accumulation of aldolase within the I-band and M-line. Therefore, the release of Ca2+ during muscle contraction might result, simultaneously, in the inhibition of glyconeogenesis and in the acceleration of glycolysis
Dans la fibre musculaire squelettique, le calcium activateur de la contraction musculaire provient d...
University of Minnesota Ph.D. dissertation. June 2011. Major: Biochemistry, Molecular Bio, and Bioph...
Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/72185/1/j.1749-6632.1988.tb33358.x.pd
<div><p>The mechanism by which calcium inhibits the activity of muscle fructose 1,6-bisphosphatase (...
The mechanism by which calcium inhibits the activity of muscle fructose 1,6-bisphosphatase (FBPase) ...
AbstractMuscle fructose-1,6-bisphosphatase (FBPase) is highly sensitive toward inhibition by AMP and...
AbstractAs our recent investigation revealed, in mammalian heart muscle, fructose 1,6-bisphosphatase...
AbstractReal-time interaction analysis, using the BIAcore biosensor, of rabbit muscle FBPase–aldolas...
AbstractAlthough it is well known that insulin controls the synthesis of glycogen from non-carbohydr...
AbstractSubcellular localization of FBPase, a regulatory enzyme of glyconeogenesis, was examined ins...
A partition equilibrium study has shown calcium ion to be a noncompetitive inhibitor of aldolase ads...
AbstractInteraction of glycolytic enzymes with F-actin is suggested to be a mechanism for compartmen...
Calcium is known to play a prominent regulatory role in skeletal muscle cells and is amongst others ...
Although it has been believed for several years that calcium ions are the means by which glycogenoly...
It is well known that exercise increases glucose transport into skeletal muscles. The regulation of ...
Dans la fibre musculaire squelettique, le calcium activateur de la contraction musculaire provient d...
University of Minnesota Ph.D. dissertation. June 2011. Major: Biochemistry, Molecular Bio, and Bioph...
Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/72185/1/j.1749-6632.1988.tb33358.x.pd
<div><p>The mechanism by which calcium inhibits the activity of muscle fructose 1,6-bisphosphatase (...
The mechanism by which calcium inhibits the activity of muscle fructose 1,6-bisphosphatase (FBPase) ...
AbstractMuscle fructose-1,6-bisphosphatase (FBPase) is highly sensitive toward inhibition by AMP and...
AbstractAs our recent investigation revealed, in mammalian heart muscle, fructose 1,6-bisphosphatase...
AbstractReal-time interaction analysis, using the BIAcore biosensor, of rabbit muscle FBPase–aldolas...
AbstractAlthough it is well known that insulin controls the synthesis of glycogen from non-carbohydr...
AbstractSubcellular localization of FBPase, a regulatory enzyme of glyconeogenesis, was examined ins...
A partition equilibrium study has shown calcium ion to be a noncompetitive inhibitor of aldolase ads...
AbstractInteraction of glycolytic enzymes with F-actin is suggested to be a mechanism for compartmen...
Calcium is known to play a prominent regulatory role in skeletal muscle cells and is amongst others ...
Although it has been believed for several years that calcium ions are the means by which glycogenoly...
It is well known that exercise increases glucose transport into skeletal muscles. The regulation of ...
Dans la fibre musculaire squelettique, le calcium activateur de la contraction musculaire provient d...
University of Minnesota Ph.D. dissertation. June 2011. Major: Biochemistry, Molecular Bio, and Bioph...
Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/72185/1/j.1749-6632.1988.tb33358.x.pd