is this stement false? Intracellular concentrations in resting muscle are as follows: Fructose-6-phosphate (1.0 mM) Fructose-(1-6)-bisphosphate (10.0 mM) AMP (0.1 mM) ADP (0.5 mM) ATP (5.0 mM) Pi (10.0 mM) Under the above conditions the Phosphofructokinase reaction in muscle is more exergonic than under standard conditions.

is this stement false? Intracellular concentrations in resting muscle are as follows: Fructose-6-phosphate (1.0 mM) Fructose-(1-6)-bisphosphate (10.0 mM) AMP (0.1 mM) ADP (0.5 mM) ATP (5.0 mM) Pi (10.0 mM) Under the above conditions the Phosphofructokinase reaction in muscle is more exergonic than under standard conditions.

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter38: The Musculoskeletal System

Section: Chapter Questions

Problem 3VCQ: Figure 38.38 The deadly nerve gas Sarin irreversibly inhibits acetycholinesterase. What effect would...

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Intracellular concentrations in resting muscle are as follows: fructose- 6-phosphate, 1.0 mM; fructose-1,6-bisphosphate, 10 mM; AMP, 0.1 mM; ADP, 0.5 mM; ATP, 5 mM; and P, 10 mM. Is the phosphofructokinase reac- tion in muscle more or less exergonic than under standard conditions? By how much?
Intracellular concentrations in resting muscle are as follows: fructose6-phosphate, 1.0 mM; fructose-1,6-bisphosphate, 10 mM; AMP, 0.1 mM;ADP, 0.5 mM; ATP, 5 mM; and Pi, 10 mM. Is the phosphofructokinasereaction in muscle more or less exergonic than under standard conditions?By how much?
Kt of glucose for GLUT1=3 mM, GLUT2=17 mM, GLUT 3=1.3 mM, and GLUT11=0.3 mM. Sketch a graph with [glucose] on the x-axis and rate of transport on the y-axis. Sketch a line for each GLUT transporter above. Which of these GLUT transporters will be working at its maximum rate at [glucose]=5 mM? Which of these GLUT transporters will be working closest to ½ Vmaxwhen [glucose]=5 mM? What will be the approximate rate of glucose transport for each of these transporters if [glucose]=17 mM?
Calculate glucose concentration. Na (sodium) and glucose secondary active transport. Na transport (which drive glucose import) G=R*T*In(Na in/ Na out)+Z*F*Y(psi symbol) Na in=14mM Na out=145MM Z=+1 F=96.5 KJ/V*mol Y(psi)=-0.05V What is the glucose in and out concentration? Please be very through when explaining this calculation. (I am stuck at why the energy sign changes from negative to positive when using the calculated energy from sodium to glucose)
What is the rationale for the inhibition of muscle glycogen phosphorylase by glucose 6- phosphate when glucose 1- phosphate is the product of the phosphorylase reaction?
Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. If ADP is five times more abundant than AMP,calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate ∆G for ATP hydrolysis at 37 °C under these conditions.The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration.
In muscle tissue, the rate of conversion of glycogen to glucose 6-phosphate is determined by the ratio of phosphorylase a (active) to phosphorylase b (less active). Determine what happens to the rate of glycogen breakdown if a muscle preparation containing glycogen phosphorylase is treated with: (a) phosphorylase kinase and ATP; (b) PP1; (c) epinephrine
Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these condi- tions. The energy charge is the concentration of ATP plus half the concen- tration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
Explain the structure of Human muscle fructose 1,6-biphosphate aldolas complexed with fructose 1,6-bisophosphate
The Vmax of muscle glycogen phosphorylase is much larger than that of the liver enzyme. Discuss the functional signifi cance of this phenomenon.
In active muscle cells, the pO₂ is about 10 torr at the cell surface and 1 torr at the mitochondria (the organelles where oxidative metabolism occurs). Calculate the percentage of bound oxygen transported to the mitochondria of muscle cells by myoglobin (KD = 2 torr). A new oxygen transport protein that exhibits cooperative binding has been isolated and is being studied in the lab. Calculate the Ko value if Y = 0.76 when pO₂2 = 18 torr (assume n = 2.5). How does this compare to the K₂ value for hemoglobin? Does this protein bind more or less tightly to oxygen compared to hemoglobin?
Intramitochondrial ATP concentrations are about 5 mM, and phos- phate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentra- tion of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]