If there are still contaminating proteins with your LDH fraction after going through 3 different purification schemes (affinity, ion exchange, and size exclusion columns), what would be their physical characteristics?
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- If there are still contaminating proteins with your LDH fraction after going through 2 different purification schemes (affinity and ion exchange chromatography), what would be their physical characteristicsIf I had a standard with 2.0 mL of Bradford reagent then added 50μL of 250 μL/mL ; what would be the concentration of original protein?A 5 ml vial of the hydrocortisone is having 2% (w/v) concentration. How many vials will be required, if we needed to prepare 30 ml of a 8 mg/ml oral hydrocortisone?
- : How can the process of hydrogenation be optimized to achieve high selectivity and conversion in the industrial production of saturated fats?The Bradford reagent gives a linear response only from 0.1 mg/mL to 1.4 mg/mL of protein concentration. Would we be able to use an "absorbance vs. concentration" line graph for samples outside of the range indicated? Justify your response.How many moles of Na2S2O3 would be required to react completely with 0.450 g of AgBr?
- Why is necessary to remove fat and tendons from the heart sample in a LDH purification experiment?Does the change Glu®Val (Eb6V) explain the unequal migration of HbA and HbS in your gel?The lipase substrate emulsion contains 0.500 mg of olive oil per 3 mL Also, the molar mass of the olive oil is 885 g/mol. If all of the olive oil in a 3 mL reaction is "digested" by pancreatic lipase in a reaction, how many molecules of olive oil have been degraded?