Measurement of beemolulose transport kinetics into oocytes in the presence of different sugars. 1) Analysis the table 2) The effect of each substrates into Km and Vmax
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Measurement of beemolulose transport kinetics into oocytes in the presence of different sugars.
1) Analysis the table
2) The effect of each substrates into Km and Vmax
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- Assessing the Effect of Active-Site Phosphorylation on Enzyme Activity (Integrates with Chapter 15.) The serine residue of isocitrate dehydroenase that is phosphorylated by protein kinase lies within the active site of the enzyme. This situation contrasts with most other examples of coa1ent modification by protein phosphorylation. where the phosphorylation occurs at a sate remote from the active site. What direct effect do you think such active-site phosphorylation might have on the catalytic activity of isocitrate dehydrogcn.ise? (Sec Barford, D., 1991. Molecular mechanisms for the control of enzymic activity by protein phosphorytation. Biochimica et Biophysica Acta 1133:55—62.)Computation: Ratio Strength, PPM, mg%Show your complete solution.1. Diabetes is diagnosed by any of the following: two consecutive fasting blood glucose tests that are equal to or greater than 125 mg/dL, any random blood glucose that is greater than 200 mg/dL, and a two hour oral glucose tolerance test with any value over 200 mg/dL.A.) what is yje equivalent value express in terms of milligrams percent?Equivalent value of 126 mg/dL in mg% = ?Equivalent value of 200 mg/dL in mg% = ?B.) how many milligrams of glucose would be present in 10-mL sample serum (use the FASTING BLOOD SUGAR LEVEL)?Calculcate Kcat for PNP substrate for both enzyme concentrations. enzyme volume: 20 ul Bovine Intensince Alkaline phosphatase molecular weight: 140,000 Bovine intenstine Alkaline phosphatase activity: 300 units/ml and 14 units/mg extinction coefficient PNP: 18.5 abs (mM-1 cm-1) Vmax: 0.332 moles/sec a) enzyme 1 concentration: undiluted b) enzyme 2 concentration: 1:1 dilution
- a) Determine kcat (in units of sec-1) for a particular enzyme, given the following information: Vo = 144 mmol/min; [S] = 2 mM; Km = 0.5 mM; Enzyme Molecular weight = 40,000 mg/mmole; 8 mg of enzyme used in assay generating this data. b) In general, explain how the total enzyme concentration affects turnover number and Vmax?ΔG°′ for the isomerization reaction glucose-1-phosphate (G1P) ⇌ glucose-6-phosphate (G6P) is −7.1 kJ · mol−1. Calculate the equilibrium ratio of [G1P] to [G6P] at 25°C.6. Reciprocal regulation of opposing pathways is necessary to avoid the wasteful synthesis anddegradation of metabolic intermediates. Provide two distinct examples of reciprocal regulation. Bespecific, and be sure to explain the conditions that signal enzyme activation and/or inhibition.
- Suggest a reason why the cell membrane of bacteria grown at 20oC tend to have a higher proportion of unsaturated fatty acids than the membranes of bacteria of the same species grown at 37oMULTIPLE CHOICE In patients with Lesch Nyhan Syndrome, purine nucleotides are overproduced and over excreted. The hypoxanthine analogue Allopurinol, which effectively treats gout , has no effect on the severe neurological symptoms of Lesch- Nyhan patients because it does not A. decrease de novo pyrimidine synthesis B. decrease de novo purine synthesis C. decrease urate synthesis D. increase PRPP levels (Phosphoribosyl pyrophosphate)Describe the endogenous mechanisms that regulate cholesterol synthesis. Want solution ASAP
- Ketosis in Dairy Cattle: 1. Explain why propionate can contribute to the next synthesis of glucose but acetic acid cant.Molecular detail of spike Y453FMany enzymes obey simple Michaelis–Mentenkinetics, which are summarized by the equationrate = Vmax [S]/([S] + Km)where Vmax = maximum velocity, [S] = concentration ofsubstrate, and Km = the Michaelis constant.It is instructive to plug a few values of [S] into theequation to see how rate is affected. What are the rates for[S] equal to zero, equal to Km, and equal to infinite concen-tration?
