Özcan MM. and his colleagues tried to obtain 3 different fatty acids from moringa pelegrina nucleus with cold pressing and soxhlet extraction by two different methods. The data is as follows; Cold pressing method Moringa pelegrina nucleus Soxhlet extraction method Moringa pelegrina nucleus Fatty acids a-tocopherol(mg/kg) 137.89 + 2.89 y-tocopherol(mg/kg) 63.68+0.87 8-tocopherol(mg/kg) 61.49+0.76 151.67+1.89 71.57+1.06 63.58+0.97 Accordingly, 3 different fatty acids obtained by 2 different methods used; a) Calculate their efficiency. b) By which method has more efficiency been achieved and explain with the reasons?

This is a visible spectra between 390-590 nm obtained during the protein separation process of haemoglobin and cytochrome c using CM Sephadex chromatography. I'd like the results shown on the image interpreted. Look for characteristic peaks or patterns that correspond to the absorption properties of these proteins in the visible range.

Does this calculation look correct? My goal isto have a target mass of 10 µg of my protein with a total volume of 30 µl. Protein was measured and found to have a concentration of at 308.35 µg/ml Recall, mass = concentration * volume 10 µg = 308.35 µg/ml * V V = 0.01 mg/ 0.30835 mg/mL = 0.032430679 mL = 32.43067942 µL Note: cannot measure this amount; two dilutions required. Dilute by 1/40: measure 2.5 µl of protein at 0.30835 µg/µl and add it to 97.5 diluent to prepare a solution of protein at 7.71 mg/ml. This diluted sample will be used further. Mass = concentration * volume 10 µg = 7.71 mg/ml * V V = 0.01 mg/ 7.71 mg/ml = 1.3 µL Therefore, will measure 1.3 µl of protein at 7.71 mg/ml and add it to 28.7 µl of diluent.

Can Hydrophobic Interaction Bead Chromatography be used to isolate Protein X from muscle tissue if Protein X contains many hydrophobic regions? Explain the process of how to isolate Protein X from muscle tissue.

A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).

5/ n SO a- 6.46 The following data show the binding of Mg2+ ions with a protein containing n equivalent sites: [Mg2+ ] total/μM [Mg2+ ]free/μM 108 Com 35 180 65 288 501 115 248 752 446 Apply the Scatchard plot to determine n and Ka. The protein concentration is 98 µM.

Please don't provide handwritten solution

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)

Please answer and explain this Biochemsitry Question to the best of your ability

Various concentrations of recombinant human insulin were prepared for use standards for an HPLC method. To verify the prepared concentrations, the samples were analyzed by measuring the absorbance at 280 nm in a short path length (5 mm) cuvette. The molar absorption coefficient for human insulin is approximately 5.875 x 10³ M-¹cm-¹. a. Calculate the extinction coefficient in mL mg-¹cm-¹. b. Calculate the concentrations of the following human insulin standards if the measured absorbances and dilutions used are: Standard 1 Standard 2 Abs. (at 280 nm) of Diluted Sample 0.305 0.685 Dilution 145.0 µL sample, 25.0 μL buffer 130.0 µL sample, 40.0 μL buffer