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Concept explainers
Interpretation:
If the chemical equation
Concept Introduction:
Statement that uses chemical symbols and formulas instead of words in order to describe the changes that takes place in a
- Correct formulas of the reactants are written in left side of chemical equation.
- Correct formulas of products are written in right side of chemical equation.
- An arrow is placed between reactants and products which point towards the products.
- If two or more substances are present in reactant and product, plus sign is used to separate them.
Balanced chemical equation is the one that has equal number of atoms of each element that is involved in the chemical reaction on both sides of the chemical equation. An unbalanced chemical equation can be balanced by adding coefficients to the equation. It is a number that is placed in left side of the chemical formula so that it changes the amount only and not the identity.
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Chapter 6 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- Match each inhibitor with its effect on Michaelis-Menten reactions. Group of answer choices Vmax and apparent Vmax are equal and the apparent Km is greater than Km. The apparent Vmax is less than Vmax and the apparent Km and Km are equal The apparent Vmax and the apparent Km are both lowered to the same degree. The apparent Vmax is less than Vmax and the apparent Km can be either greater than or less than Km.arrow_forwardA doctor wants to prescribe a 70 kg patient a drug to be taken PO. In order to achieve an average steady-state plasma concentration (Css) of this drug in its therapeutic range, the patient needs to have a of Css of 597 μg/L. The VD of this drug is 2.3 L/kg, the F of this drug is 0.70, and the half-life of this drug is 12.9 hours. What is the necessary dosing regimen needed to achieve the desired Css? (units: mg/day, i.e., mg/24 h))arrow_forwardAcetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vmax) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 (S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (*"A JO %) Aarrow_forward
- Define the following terms:a. allyl groupb. epoxidec. SAM d. PAPSe. phase I reactionarrow_forwardGiven the equation of the line, y=150x-8.1221 (cells per mL is in 10^8), what is the CFU per mL of the original suspension if the thousand-fold dilution of that suspension has an absorbance of 0.3 at 600nm? * A. 3.7 x 10^12 B. 3.7 x 10^9 C. 3.7 x 10^1 D. None of these is correctarrow_forwardQuestion 23 An enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation... SHOW MORE V The Km for X will be affected if Y is present in the reaction mixture. a Y is a competitive inhibitor of X. The Km for X will increase. d. The V for X will be affected if Y is present in the reaction mixture. max pH dependence of Vmax reflects the ionization state of catalytic site e residues. Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X = 0.01 M and the Km for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of g products to reactants (Keg).arrow_forward
- A patient presents to the emergency department in a critical condition. The patient’s blood was tested and the concentration of carbonic acid (H2CO3) was found to be 4.0×10-4 M and bicarbonate ion (HCO3-) 3.062×10-3 M. Ka = 4.3 × 10-7 H2CO3(aq) ⇌ HCO3-(aq) + H+(aq) Show all calculations including equation(s) used. Calculate the pH of the patients’ blood. Based on your answer would you say the patient is suffering from Acidosis or Alkalosis?arrow_forwardThe conversion of glucose-1-phosphate to glucose-6-phosphate by the enzyme phosphoglucomutase has a △G°' of -7.6 kJ/mol. Calculate the equilibrium constant for this reaction at 298 K and a pH of 7. (R = 8.315 J/K-mol) A. 0.003 B. 0.047 C. 1.00 D. 21arrow_forwardFigure I shows the Michaelis Menten plot of initial reaction velocity (as percentage of Vmax) versus [S] (concentration) for the carbonic anhydrase reaction in the absence and presence of the inhibitor acetazolamide. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. 100 No inhibitor Acetazolamide 0.2 0.4 0.6 0.8 1 [S] (mM) Figure 1 (i) Compare Vmax and Km of the enzyme without inhibitor and in the presence of acetazolamide. Determine the type of inhibition shown by acetazolamide. Explain your answer. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide in Qla)(i). List down the kinetic properties of these inhibitions. Sketch a graph of I/V versus 1/[S] showing plots in the absence of an inhibitor and in the presence of the types of inhibitors mentioned in Qla)(ii). (iii) V (% of Vmaxarrow_forward
- At 39.9ºC, a solution of ethanol (XetOH = 0.9006, P * etOH = 130.4 Torr) and isooctane (P * iso = 43.9 Torr) forms a vapor phase with YetOH = 0.6667. The total pressure is 185.9 a. Calculate the activity and the activity coefficient of each component.b. Calculate the total pressure the solution would have if it were ideal.c. Comparing the ideal pressure to the actual pressure, what does this indicate about the molecular interactions?arrow_forwardWhat is the concentration of B expressed in terms of A if the Kd is 33.0 uM, and the concentration of AB is 56.0 uM? A + B AB OB= 1850/A OB= 23 - A OB=23+ A OB= 0.589/Aarrow_forwardFind the Gibbs free energy of mixing when 2 moles of ethanol is mixed with 5 moles of water at a temperature of 27 °C. The pressure of the system is kept constant. The two liquids form an ideal solution. O A. -10.45 J O B. 10.45 kJ O C. -11.75 kJ O D. 11.75 kI O E. -10.45 kJarrow_forward
- Essentials of Pharmacology for Health ProfessionsNursingISBN:9781305441620Author:WOODROWPublisher:Cengage