Hexokinase in red blood cells has a Km of approximately 50 µM. Whatconcentration of blood glucose would yield a velocity equal to 90 % Vmax?Select an answer and submit. For keyboard navigation, use the up/down arrow keys to selectan answer.a500 mM0.0450 mM4500 μΜ5000 µMe5.0 mM0.50 mM450 μΜ4.5 mM50 μΜ.

Answered: Image /qna-images/answer/8d246064-cdd3-4e21-8aea-d6aba91cf141.jpgThe concentration of blood glucose is = 450 micro Molar. So option E is correct

Answered: Hexokinase in red blood cells has a Km…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Similar questions

The units for the unimolecular reversible rate constant for the forward reaction are ○ M sec-1 sec M-1 sec-1 sec-1
You have an initial solution in which you added quantities of “A” and “B” such that there is 4.5 M “A” and 2.5 M “B” and no complex (“AB”) at time 0. After equilibrium, you are able to isolate and quantitate the “AB” complex, and find its concentration is 1.5 M. Given that RT is 0.59 kcal/mol, what is the delta Go’ for the association reaction?
Calculate the actual free energy of hydrolysis of ATP, delta Gp in the erythrocytes of a new species. The standard free-energy of hydrolysis of ATP is also -30.5kJ/mol in this species, but the concentrations in this specie's erythrocytes are 0.00760 mM ATP, 0.00063 mM ADP and 0.00273 mM Pi. Assume the pH is 7.0 and the body temperature of this species is 91.0oC. Calculate your answer as kJ/mol to two decimal places.
A one-to-one protein (P)-ligand (L) complexation (P + L PL) has a dissociation equilibrium constant (Kd) value of 100 nM at 25°C, and the Kd remains the same at 37°C. 1) What is AS of binding at 25°C? Assume ACp of the binding is 0 over the temperature range. AS = 1.34E2 kJ/(mol*K) (note the unit!!) (sig. fig =3) 2) What is the concentration of the PL complex formed at equilibrium when you mix 0.20 uM (microM) of Protein and 1.0 uM of Ligand together at 37°C? PL at equilibrium = 8.1E-1 uM (note the unit!!) (sig. fig =2)
8L.3.4
In considering active transport by Na + -K + -ATPase at body temperature (37 o C), 3 Na+ are pumped out of the cell and 2 K + are pumped in for each ATP that is hydrolyzed to ADP + P i . Given that underyour experimental conditions, the DG for ATP hydrolysis is -10 kcal/mol, and that V is -60 mV, and that the pump maintains the internal Na + at 10mM, external Na + at 120 mM, internal K + at 120 mM and external K + at 8mM, what is the efficiency of the pump (i.e., what fraction of the energy available from ATP hydrolysis is required to drive transport at the provided levels)?
Please note when values are from an external source/table. List any assumptions.
The free energy of hydrolysis for acetic anhydride is221.8 kJ/ mol. The conversion of ATP to ADP also involvesthe cleavage of an anhydride bond. Its free energy of hydrolysis is 230 kJ/ mol. Explain the difference in these values.
The Nutrition Facts label on most food products shows % daily values based on a food energy requirement of 8,360 kJ (2,000 kcal) at normal resting state. a) Assuming that the efficiency of converting food energy to ATP is 50%, calculate the mass of ATP (in kg) that is harvested daily by the human body from 8,360 kJ of food energy. A total of 30.5 kJ of energy is needed to synthesize one mole of ATP under standard conditions. The molar mass of ATP is 505 g/mol. b) For an average 68-kg (150 lbs.) human adult, calculate the % mass of extracted ATP (from your answer in 2a) relative to body weight.
In a alkaline phosphatase kinetics experiments a studnet first made a standard curve with different amounts of PNP. In a reaction carried out with 10nM alkaline phosphatase and 100 uM PNPP substrate the student measured an absorbance value of 0.76 at 410nm after 30 seconds of reaction. Assuming the 30 second time point is in the lienar range of the reaction and the substrate has not been depleted at this time point, calculate the Vo at 100uM PNPP (in units of concentration per time).Beer's law formula given is y=0.0323x (y axis is Absorbance) (x Axis is PNP uM)
The hexapeptide Ala-Met-Leu-Lys-Phe-Asp is digested in the same tube with both Cyanogen Bromide and Trypsin at the same time at pH=7. Draw the structure of the product(s) that would bind to a cation exchange column. (Relevant pKa values are 2.2, 3.9, 9.5 and 10.5. Assume pKa values for any newly generated a-amino and a-carboxyl groups are 9.5 and 2.2 respectively)
Twenty-three milligrams of glucose were eaten by the bacteria Sanacoccus pumasareus. Calculate the hypothetical amount of ATP your patient can generate under aerobic respiration with this amount of glucose. (Note: Glucose MW-180.16 g/mole; 1 mole= 6.02 x 1023 molecules (Avogadro's number)). 2.8 x 10^24 ATPs 02.9 x 10^21 ATPs 028 x 10-21 ATP5 029 x 10 24 ATPS Lacks information, cannot be determined

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS

Hexokinase in red blood cells has a Km of approximately 50 µM. What concentration of blood glucose would yield a velocity equal to 90 % Vmax?