1. Lactoferrin is an iron-binding glycoprotein that forms the antibiotic fragment lactoferricin during digestion. The protein was isolated from 1.5 liters of ewe skim milk by successive ammonium sulfate precipitation until a final salt concentration of 70% was obtained. Determine the amount (in g) of powdered ammonium sulfate needed in bringing the solution from (a) 0% to 40% saturation and (b) 40% to 70% saturation assuming that the volume remains constant.

1.0 0.9 Z 0.8 15. A pharmaceutical company studied the binding of three different compounds, X, Y, and Z, to a particular protein of interest. For each compound, the fractional saturation (v) was determined as a function of concentration. The results are shown in the figure. Which of the three compounds has the strongest affinity for the protein? Explain. 0.7 X 0.6 > 0.5 0.4 0.3 0.2 0.1 0.0 Y 0.0 0.2 0.4 0.6 0.8 1.0 1.2 1.4 1.6 1.8 2.0 2.2 2.4 2.6 2.8 3.0 L(μM)

Given a stock protein solution with a concentration of 6 mg/ml, determine the protein concentration of a solution made by mixing 5 μl of the stock with 5 μl of a buffer.

1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:

2.58. Bacteria have equivalent diameters of 2 × 10-6 m and densities of approximately 1 kg/L. Under optimal conditions, bacteria can di- vide every 30 min. Determine the mass of bacteria that would accumulate in 72 hr under continuing optimal growth conditions. Can this occur? Explain.

calculate the volume of stock solutions required to make up the buffer solutions that will be used for protein purification. The solutions you need to prepare for purification are: i. Binding Solution A: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 5mM imidazole, 5% (v/v) glycerol ii. Wash Solution B: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 75mM imidazole, 5% (v/v) glycerol iii. Elution Solution C: make up 10 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 500 mM imidazole, 5% (v/v) glycerol please show your working . Thnk you

A stock solution contains 0.2 mg/mL protein. From this stock solution, 179 uL is diluted with 1.1 mL buffer. What is the concentration of protein in this dilution?

The α-amylase (α-AM) enzyme secreted by Aspergillus has an isoelectric point of approximately 4.2. If the purification method in problem 1 operates at pH 6.5, would the protein carry a positive charge, negative charge, or net zero charge?

you are ready to elute your MBP-BAP protein from the column using 1.5mL of TBS + 10mM maltose. Create a buffer from the provided 1x TBS and 500mM maltose stock solution.

Which of the following is NOT a unit of concentration?     All of these options are units of concentration.     mM     Moles/Liter     Molar   You gathered your data from Lab , and found the following values: Total Activity of lysozyme in HEW: 14 units Total Activity of lysozyme in carb 1: 21 units Total amount of protein in HEW: 70 mg Total amount of protein in Carb 1: 15 mg Calculate the extent of purification of lysozyme in Carb 1. A   7 fold B   150% C   15 fold D   70%