A cyclic AMP (CAMP) binding protein was isolated from mammalian cells and characterized by equilibrium dialysis experiments (data are shown below). This protein was present in the dialysis bags at 16 µM. i) ii) iii) Concentration of CAMP (μM) Outside bag 0.7 2.3 4.5 10.0 30.0 70.0 150.0 Inside bag 2.7 8.3 15.0 26.0 54.0 98.0 180.0 Using a Scatchard plot, estimate the Kd for the CAMP. Estimate the number of biding sites per protein molecule. What other information could be obtained from this analysis?
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- Cimetidine is used in the treatment and management of gastric ulcers and gastroesophageal reflux disease. In the case of an active ulcer, cimetidine can be administered continuous by IV infusion at a dose rate of 37.5 mg/hr. If the concentration of the cimetidine solution is 6 mg/ml, then how many milliliters must be available for a 4-hr infusion?Misoprostol is used to prevent NSAID-induced gastric ulcers. A daily dose consists of two tablets administered four times each day. What is the size of one day’s dose if each tablet contains 100 mcg of misoprostol?What is the approximate rate of change of A340 measured? i.e. ΔA340 / min = __________ What rate of change of A340 would you predict if 30 ml of the ADH solution was tested in the same way (i.e. half the amount of protein) ? i.e. ΔA340 / min = __________ What rate of change of A340 would you predict if 60 ml of a 0.5 μM ADH solution was tested in the same way? i.e. ΔA340 / min = __________ As well as writing your answers, explain your reasoning.This graph represents a standard curve from a BCA assay for protein concentration. If your BCA reaction with your unknown protein has an absorbance of 0.2, approximately what concentration of protein is in your unknown sample? Absorbance (562nm) 0.5 0.45 3 0.35 0.3. 0.25 0.15. 0.1- 0.05 ~0.1 μg/ml ~4.5 μg/ul less that 0.005 | 0.2 μg/μ. [Protein (BSA)) (pg/ml)
- Given this, if you used 6g of vitamin Z powder to make 20 ml of solution, what is the % concentration of this solution? (I gave the image since I don't know if that info is needed to solve this question.)It also gives a follow-up, if you can help here too: You work in a lab as a summer student. One of your tasks is to make sure that there is enough cell culture medium containing antibiotics to grow bacteria. One day you realize that there is only 5 ml of 10% Antibiotic stock solution in the freezer. You decide to use it all to prepare the working culture medium with 0.01% antibiotic. In the lab there is plenty of growth medium without antibiotics. (Note: dilution in medium is like dilution in water). You remember the equation to make dilutions of stock solutions. You usually use this formula to calculate the required volume of a stock solution, but you realize it can apply here as well, even though the unknown is the final volume. So, you make that dilution. Given that each bacterial…Paclitaxel is used to treat ovarian cancer by infusion at a concentration of 0.6 mg/mL over 24 hours. A dose of 135 mg/m² has been prescribed for Sero. Sero is 1.06 m tall and weighs 92 kg. Paclitaxel comes in vials of 150 mg/25 mL. Calculate the volume of 5%w/v glucose solution that would be required to dilute the concentrated solution to prepare an paclitaxel solution of the required strength.Paclitaxel is used to treat ovarian cancer by infusion at a concentration of 0.6 mg/mL over 24 hours. A dose of 135 mg/m² has been prescribed for Sero. Sero is 1.06 m tall and weighs 92 kg. Paclitaxel comes in vials of 150 mg/25 mL. Calculate the volume of 5%w/v glucose solution that would be required to dilute the concentrated solution to prepare an paclitaxel solution of the required strength. Answer: You did not give the correct unit. The correct answer is: 333 mL X
- We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: I- *H₂N- glutamate H - C-COO CH₂ CH₂ COO 0.1 M phosphate buffer pH 7.4 : 550 μL 1.2 M alanine: 100 μL CH3 pyruvate CH3 C time (min) A340 CIO O COO The enzyme reaction is alized in the following conditions: In a 1 cm-cuvette are added: COO™ pyruvate lactate dehydrogenase* (LDH, 300 µμg.mL-¹): 50 μL 1.5 mM NADH : 200 μL 0.04 M a-ketoglutarate: 500 µL serum containing ALAT: 600 μµL ALAT NADH + H+ 0 0.915 a-cétoglutarate COO LDH * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. с=0 CH₂ 1 0.741 Reaction 2: NAD+ CH₂ COO™ H-C CH3 OH COO™ lactate alanine H + *H3N-C The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: ENADH at 340 nm =…On the right the Hill plot com- (b) pares the O2 binding properties of Hb Ya- kima with those of HbA in 0.1 M NaCl buff- Hb-Yakima ered to pH 7 with 0.01 M bis-Tris. Focus first on the line for "stripped Hb". This is the term for hemoglobin isolated from erythro- cytes with removal of all organic phosphate molecules that might bind to the protein in RBCS. You can see that 2,3-bisphospho- glycerate (BPG; labeled DPG according to old terminology) does not alter the O2 bind- ing affinity of Hb Yakima in contrast to HbA (although it was shown that BPG did bind to the deoxyHb Yakima molecule). Also, Hb Yakima is associated with markedly decreased allostery in the absence and presence of BPG, in comparison to HbA. IHP = inositol hexaphosphate, an artificial allosteric modifying ligand that binds more tightly than BPG. stripped Hb Hb-A •DPG +DPG n= 1.0 n = 2.3 n=2,5 +THP +IHP 0.5 0.5 1 5 10 50 po, ( mm Hg ) %3D On the right is a diagram copied from the lecture handout "Hemoglobin and Allo-…We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: +H3N- glutamate H C CH₂ CH₂ COO -COO + pyruvate CH3 C=0 0.1 M phosphate buffer pH 7.4 : 550 µL 1.2 M alanine : 100 μL CH3 time (min) A340 COO COO™ pyruvate lactate dehydrogenase* (LDH, 300 µg.mL-¹): 50 μL 1.5 mM NADH: 200 μL 0.04 M a-ketoglutarate: 500 μL serum containing ALAT: 600 μL The enzyme reaction is realized in the following conditions: In a 1 cm-cuvette are added: 0 0.915 ALAT NADH + H+ LDH a-cétoglutarate COO * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. Reaction 2: NAD+ 1 0.741 C=O H CH₂ CH₂ COO™ CH3 C-OH COO lactate The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: alanine ENADH at 340 nm = 6220 M¹.cm1. One…
- Penicillin is hydrolyzed and thereby rendered inactive by penicillinase, an enzyme present in some resistant bacteria. The mass of this enzyme in Staphylococcus aureus is 29.6 kd. The amount of penicillin hydrolyzed in 1 minute in 10 ml solution containing 10–9 g of purified penicillinase was measured as a function of the concentration of penicillin. Assume that the concentration of penicillin does not change during the assay. [Penicillin] µM Amount hydrolyzed (nanomoles) 1 0.11 3 0.25 5 0.34 10 0.45 30 0.58 50 0.61 a) Plot V0 versus [S] and 1/V0 1/[S]. Does penicillinase appear to obey Michaelis-Menten kinetics? b) What is the value of KM? c) What is the value of Vmax? d) What is the turnover number of penicillinase under these conditions?A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).From this standard curve and chart below, does the separation of molecules in the mixture appear successful from the gel filtration? Is there a clearlydefined separation between molecules? Explain your conclusions. Parameters required for calculation of coefficient (Kd) for unknown protein Volume eluted (mL) Which variable does this volume represent in the equation for Kd? Fraction with maximal DNP-Aspartate detected 36 Vt Fraction with maximal Protein detected 24 Ve Fraction with maximal Blue dextran detected 6 Vo