Calculate the specific activity and kcat for this enzyme
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- The initial velocity data shown in the table were obtained for an enzyme. Each assay at the indicated substrate concentration was initiated by adding enzyme to a final concentration of 0.01 nM. Derive Km, Vmax, kcat, and the specificity constant. [S] (mM) Velocity (x10^7) 0.10 0.96 0.125 1.12 0.167 1.35 0.250 1.66 0.50 2.22 1.0 2.631 pt pt 9146 Bb 9146 Bb 1031 Class Etsy E Traps E Traps New Free Chat + ☆ 出口 keAssignment/takeCovalentActivity.do?locator-assignment-take [References] You do an enzyme kinetic experiment and calculate a Vmax of 118 μmol per minute. If each assay used 0.10 mL of an enzyme solution that had a concentration of 0.20 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol? (Enter your answer to two significant figures.) turnover number = sec-1 D 1 pt Submit Answer Try Another Version 2 item attempts remaining estion stion 5 on 6 7 1pt 1 pt 1 pt 1pt 1pt 1pt 1 pt 1 pt D is the substrate concentration multiplied by the catalytic constant. KM is equivalent to the substrate concentration multiplied by the ratio of rate constants for the formation and dissociation of the enzyme-substrate complex. KM is equivalent to the substrate concentration. KM is equivalent to the substrate concentration divided by 2 A: KM is equivalent to the substrate concentration…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).
- Calculate the Activity of an amylase enzyme which is diluted 1:100 times with phosphate buffer and incubated for 10 minutes at 37 degree Celsius. Given are the amount of maltose [mg] = 5.05 and the volume of enzyme used for the assay as 0.5ml.Identify the most cost effective enzyme purification method and provide brief explanations for this method. ▪Repeated freezing and thawing ▪Sonication ▪Homogenization by high pressure (French press) ▪Homogenization by grinding (bead mill) ▪Permeabilization by detergents (e.g. Triton X-100) and/or enzymes (e.g. lysozyme)(A) Below is a partial purification table for a first attempt at a purification schedule for an enzyme: Technique Initial IMAC IEX Gel Filtration Protein (mg) 3467.8 196.7 153.6 142.1 Enzyme activity (units) 36489 32575 27891 26398 Overall yield (%) 100 Specific activity (units/mg) 29.46 Complete the table below by calculating the missing values. Overall Enrichment 1.00
- Briefly comment on the differences of using a fixed-time assay versus a kinetic assay to measure enzyme activity. Is it reasonable to assume that the reaction velocity obtained by measuring the amount of product after 30 minutes in a fixed-time assay is directly proportional to absorbance? How could you determine whether this was the case? Word limit 180 words including citation and referenceYou are interested in purifying an enzyme X and decide to use an affinity chromatography followed by an enzymatic assay. You obtain the following data: Total volume of [protein] the sample (ml) (mg/mL) (U) |Total activity Sample name Specific activity |(U/mg) |Affinity | chromatography 2 0.12 5000 20833 You have obtained a 10X fold purification and a yield of 10% at the Affinity step. What was the protein concentration of your crude lysate sample, if its volume was 15 mL? Detail your answer by showing the calculations, and do not forget the UNITS!What is the need of adding DNS solution to the enzyme substrate solution bWhat is the problem in determining rates at low substrate concentration? c. Calculate the Activity of an amylase enzyme which is diluted 1:100 times with phosphate buffer and incubated for 10 minutes at 37 degree Celsius. Given are the amount of maltose [mg] = 5.05 and the volume of enzyme used for the assay as 0.5ml.
- 200 ml of a 2% protein solution are available, containing an enzyme to be purified. Half of the sample is subjected to method A, consisting of fractionated precipitations, and 5 ml of final solution are obtained, with a protein concentration equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml is obtained, with a protein richness equal to 10 mg / ml, and with an enzymatic activity equal to 2000 U / ml. You want to know: a) Which of the methods has provided the purest enzyme. b) By which of the methods has the greatest amount of protein been obtained.The diffusivity of amino acids in polyacrylamide gel is approximately 1x10^-9 cm2./s calculate the initial flux of amino acids, give an instantaneous gradient of (20g/cm 3 )/8cm Why is polyacrylamide gel is used in electrophoresis?You have performed protein purification on your new favorite enzyme using a protocol which involves the following steps/samples: crude extract, ammonium sulfate cut, ion exchange and gel filtration. You need to run 25ug of protein from your crude extract sample on an SDS-PAGE gel. You have determined that the protein concentration of your crude extract sample is 2.1mg/ml. Your total sample volume is 30ul. You have water for your diluent and 6x SDS-loading dye to prepare your sample. List the components of your prepared sample. Note: you will only have access to a P20 and a P200 to prepare this sample.