![al keat = 195 st · [E] in molly 0.3 0.35 mg in imL q xom (V = 0.3m2) =) mass = (0.357 mo. moles : 0.105 x1099 1.4x10 = 0.105n](http://img.homeworklib.com/questions/f5a99d30-d111-11eb-a9f2-794cf419e408.png?x-oss-process=image/resize,w_560)
I have already calculate the catalytic efficieny. Please calculate the Vmax and show work. 1. (10...
1. The following kinetic data was generated for the Hst enzyme. The overall reaction for this enzyme is: OH ОН + NH3 NH2 All reactions are carried out in a final reaction volume of 2 mL with 0.1ug of purified Hst protein present at pH 7.8. The Hst protein has a molecular weight of 90 kDa based on estimates from gel filtration column chromatography and a molecular weight of 45 kDa based on estimates from denaturing SDS PAGE gel electrophoresis....
12)Show work step by step
13)Show work step by step
Below is BoX 6-1 if needed
Applying the Michaelis-Menten Equation IV An enzyme is found that catalyzes the reaction X= Y Researchers find that the Kyn for the substrate A is 4 pm, and the keat is 20 min . (a) In an experiment, (X) = 6 mm, and the initial velocity, V, was 480 nm min!. What was the (E) used in the experiment? (b) In another experiment, (E)...
Determine the kinetic parameters, Km & Vmax and calculate
k2.
Penicillin is hydrolyzed and thereby rendered inactive by penicillinase, an enzyme present in some penicillin-resistant bacteria. The mass of this enzyme is 29.5 kD. The amount of penicillin hydrolyzed in 1 minute in a 10 mL solution containing 100 g of purified penicillinase was measured as a function of the concentration of penicillin. Assume that the concentration of penicillin does not change appreciably during the assay. (a) Plot v versus....
please show work so i can understand any mistakes I may have made if any. I will kindly rate. Round your answers to two or three significant figures, as appropriate. 1. For a Michaelis-Menten deacetylase with a Ks for substrate binding of 2.6 x µM, half maximal velocity is achieved with a substrate concentration of 2.8 µM. a. What is Km for the deacetylase and what kind of kinetics does this enzyme follow: rapid equilibrium or just the general steady...
how do you make a lineweaver-burk plot where the trend line
extends backwards? is there a way of figuring out how far back it
should extend based of your data ? As well, how do you plot two
sets of data on one graph ? Thank you! (idk if you need to see my
data-> attached below)
Biochemistry Enzyme Kinetics Assignment Four answers for this assignment will be completed in elearn: En in elearn: Enzyme Kinetics Quiz ots but must...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A↽−−⇀B. For substrate A, she determined that ?m=2.5 μM and ?cat=35 min−1. Jessica graduated and her project has been passed on to you. Unfortunately, Jessica was so busy that she sometimes forgot to record all of the details of an assay in her lab notebook. Your mentor suggests that you try to back calculate some of the missing concentration values. Assume that the enzyme follows Michaelis–Menten kinetics. 1)...
1. Please calculate for the missing mmol and equivalents and
show your calculations.
2. Use 3g of 3-nitrophthalic acid and the new equivalent values
to determine what quantities of reactants and solvents are needed
for the specific mass of 3-nitrophthalic acid given. Please show
your calculations.
Reactant or Solvent d (g/mL) or M(mol/L) Molecular Weight (g/mol) Reaction Weight (g) or Volume (mL) mmol Equivalents 3-Nitrophthalic Acid NA 211.13 1.00 g 4.74 mmol 1.00 32.05 2.00 mL mmol Hydrazine (8 wt%...
I only need help with part D. The answer is
0.065 sec-1, but I need help to understand why.
You are studying a dehydrogenase enzyme that catalyzes the formation of NADH from NAD^+. Subsequent studies determined that NADU will absorb at 340 nm while NAD^+ will not. The extinction coefficient for NADH is 6220 M^-1 cm^-1. The reaction volume is 750 mu L total and the substrate molecular weight is 223 g/mol. You used 20 mu L of enzyme from...
please show work
so: 1 ml stock 10 ml final -0.5 mL of stock -5 ml final volume While I have used 1:10 as a standard the same rules apply for all dilution factors. Try these problems: x 0.5 X0.5 1. You need to make a 1:25 dilution factor. If you final volume is 25 mL this means that you need_ _mL of stock and mL of solvent to make your final volume of 25 mL. 2. If you needed...
1. Calculate the pKa of lactic acid, given that when the concentration of lactic acid is 0.010 M and the concentration of lactate is 0.087 M, the pH is 4.80 B. Calculate the ratio of the concentrations of acetate and acetic acid required in a buffer system of pH 5.30 C The pH of a 0.20 M sodium acetate buffer is 5.1. The pKa of acetic acid is 4.76. Explain in details (showing all calculation) how to prepare the buffer...