Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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You are super jazzed because your protein is purified and at a concentration of 600 μg in 1.75 ml of buffer.
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Convert this concentration to mM. Note that biochemisfunase has a molecular weight of 54,321 Daltons (which is just another unit for g/mol). Show your calculations.
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- Mike has determined that enzyme he is attempting to purify has an isoelectric point of 4.5 (pI = 4.5). He has decided to examine anion exchange chromatography as a potential purification step. He tested out using 2 different buffer and linear NaCl gradient on HPLC (like what you did). His results are shown below. Which buffer should Mike uses for his purification (both buffer has pH higher than enzyme’s pI)? Why?arrow_forwardPrepare a schematic diagram and present it as though it were a Figure in a publication (scientificjournal or textbook) (20%). The Figure should illustrate the interactions made between thekey components of (a) total and (b) non-specific binding reactions. In preparing your figure,you should reflect on the role of each of the components of the reaction mixtures, and whythe subtraction of non-specific from total binding allows us to calculate specific binding.arrow_forwardDo not give handwriting solution.arrow_forward
- Acetic acid is the principal ingredient in vinegar as shown; that's why it tastes sour. At equilibrium, a solution contains [CH3CO2H] = 0.0787 M and [H3 O+] = [CH3 CO2−] = 0.00118 M. What is the value of Ka for acetic acid?arrow_forwardDuring successful purification of every enzyme, the following may be expected: Select ALL that apply. 1. Solubility in NaCl increases 2. The activity increases 3. The specificity increases 4. The number of subunits increases 5. the epitope number increasesarrow_forward200 ml of a 2% protein solution containing an enzyme that you want to purify. Half of the sample is subjected to method A, consisting of fractionated precipitations and 5 ml of final solution are obtained, with a concentration protein 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, with protein richness equal to 10 mg / ml and with an activity enzymatic also equal to 2000 U / ml. You want to know: a) Which of the two methods has provided the purest enzyme. b) By which of the methods the greatest amount of enzyme has been obtained.arrow_forward
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