9. The following proteins were identified in a mixture. protein te precipitate MW (kDa) 4.8 22...
Work out 9C and 9D using info given please. No additional info is needed. Workout all parts of number 9. Explain in clear details on how to draw a gel, why and how to determine where the bands will be formed. 9. The following proteins were identified in a mixture. protein MW (kDa) 38 4.8 [MgSO.) resured to precious 45% 80% 65% 20% 30% 45% 6.8 9.50 5.3 115 a) What is meant by "salting out a protein using MgSO:?...
You have a mixture of three proteins: Protein X, MW 15 kDa, pI 4.5 Protein Y, MW 25 kDa, pI 8.5 Protein Z, MW 75 kDa, pl 5.0 2) You have a cation exchange (acidic) column, low salt (100 mM NaCl) and high salt (1 M NaCI) buffer at pH 7.0. If you loaded the above mixture of proteins on the column in low salt buffer, which proteins would most likely be retained on the column? If you loaded the...
NOTES: To separate on a size-exclusion column, differences in MW need to be greater than 10%. To separate proteins by charge, the difference in pI must be at least 0.5 pH unit. Consider the table of four proteins below: Protein Size pI Size exclusion Charge at pH 7.4 DEAE-elution 1 49 kDa 6.8 2 51 kDa 8.1 3 53 kDa 6.4 4 99 kDa 8.3 5 106 kDa 3.8 6 143 kDa 7.9 (a) In what order would the proteins...
6. You are given a mixture of proteins that you analyze by standard 2-D electrophoresis, with the following results for isoelectric points and apparent molecular weights: protein A (Mr 110,400; pl 4.60), protein B (Mr 10,100; pl 6.93), protein C (Mr 65,200; pI 7.84), and protein D (M 25,000; pI 8.15) a. After the 2-D separation, which protein will be in the upper left quadrant of the gel. given that e cathode-proximal end of the isoelectric focusing gel was on...