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3. Scientists working on developing better resins than Sephadex have come up wit

ID: 166980 • Letter: 3

Question

3. Scientists working on developing better resins than Sephadex have come up with two new resins to be used for gel filtration chromatography, one that is very good at forming hydrogen bonds with a variety of molecules, and one that has a net charge of +3 per subunit of the resin polymer (i.e. is highly positively charged throughout the resin). (i) Do you think that these will be useful for gel filtration chromatography? (3 marks) (ii) How might your own gel filtration chromatography experiment be different when using each of these resins? Explain your answer based on the properties of each of the molecules you are separating using gel filtration chromatography. (3 marks)

Explanation / Answer

Q.No I

Hemoglobin and myoglobin will be used for the gel filtration chromatography. Any time a gel filtration material is placed in an aqueous solution it swells. How much bloating relies on the degree of cross-linking connected with the material; the low this crosslinking the greater bloating along with the more fragile the gel will be. After a gel has been equilibrated in a starting buffer it is usually put directly into a column and permitted to settle. Any time a concoction of compounds is granted to give the column filled together with the gel, the compounds will pass through directly into the gel matrix in an amount ruled by simply the molecular weights. Because buffer is usually handed as a result of the column the compounds will become lost by the size. The smaller a substance is usually, the more it will likely be stored about the column.

Q.No 2

Myoglobin is an oxygen-storage component. We have a close chemical type likeness between myoglobin and haemoglobin, the oxygen-binding protein of red blood cells. Both of these proteins contain a molecular constituent known as heme, which can enables them to combine reversibly with oxygen. This heme group, which contains iron, imparts a red-brown colour to the proteins. The molecular weight of myoglobin is 16,952 Da and it can separate the proteins in gel filtration chromatography.

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