Use the diagram below to answer the following question. Identify the protein that was run on Mass Spec? (HINT: You will need to look up the molecular weights) Relative Abundance, % 800 Human IgG Casein ESI MS Pepsin 18+ 15+ 16+ 1200 Cyanogen bromide 14+. 13+ m/z 12+ 11+ 1600 23,984 +/-2 10+ 1400 1410 1420 9+ 24,024 +/-2 2000 24,093+/-2 8+
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- The following list of proteins are found in a mixture and are to be separated by 2D gel electrophoresis: Molecular weight (Daltons) Protein Isoelectric point Myoglobin 17,000 7.0 Cytochrome C 12,000 10.6 IgG 150,000 6.4 Hemoglobin 64,500 7.1 Insulin 5,800 5.4 Human serum albumin 66,000 4.6 Histone H3 15,000 10.8 Рepsin 33,000 1.0 In 2D electrophoresis, the mixture is first subjected to isoelectric focusing, separating them via their isoelectric pH values (corresponding to the horizontal axis, then subjected to SDS-PAGE to separate via molecular weight (corresponding to the vertical axis), where large proteins stay at top and smaller proteins go towards the bottom. 2 4 pH 7 10 direction of electric current 150 MW (kDa) 100 В E A 50 2 4 pH 7 10 With this information, match the letters of the bands to the proper protein based on the data given. Band Letter Protein A D EThe proteins given below are separated using CM cellulose at pH 7.0 Write the order of elution of these proteins from the column Proteins pl Fibrinogen 5.8 Hemoglobin 7.1 Lysozyme 11.0 Pepsin 1.0 Ribonuclease 7.8Leni, Isko and Ping are trying to determine the molecular weight of their crude protein samples using SDS-PAGE. After running their samples, they obtained the following bands in their gel. Ladder Leni Isko Ping 1200 Da A 1000 Da 900 Da C 800 Da 700 Da F 600 Da 500 Da 400 Da 300 Da 200 Da 100 Da H Dye front a) Which protein/s is/are present in Leni's sample but not present in Isko and Ping's sample? b) Which protein/s is/are present in Isko's sample but not present in Leni and Ping's sample? c) Using the regression line, calculate the molecular weight of each protein subunits (A-H). |- |- |- 001 2 3 4. 6. 10
- Four proteins Cytochrome C (pI=10.2) Myoglobin (pI=7.2), Hemoglobin (pI = 6.8) and Serum Albumin (pI= 4.8) were used in our gel electrophoresis lab exercise. If the electrophoretic separation is carried out at pH 7.0, which protein would move toward the negative electrode? Cytochrome C Myoglobin HemoglobinFigure 3: ● ● ● ● ● ● KDa ● 97.4 66.2 45.0 ● 31.0- 21.5 14.4 S-1 p-1 S-2 2-0 This figure was generated by centrifuging a pura sample of protein, removing the supernatant, and resuspending the pellet in the same volume as the supernatant to allow direct comparison. The supernatant and pellet samples were then prepared for SDS-PAGE identically and run via normal SDS-PAGE procedures. In the figure, "s" means supernatant and "p" means pellet. The text or number after the dash represents a different condition. For example, s-1 and p-1 are the supernatant and pellet samples under condition 1. It is not shown, but under wild-type conditions, essentially all of the protein is found in the supernatant. S-3 ● What does the intensity of each band represent? ● Would you find soluble protein in the supernatant or pellet? Why? Would you find aggregated protein in the supernatant or pellet? Why? For each condition (there are 5 different conditions), is there a higher percentage of the total protein…Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen 6.6 115 Hemoglobin (monomer) 7.1 16 Myoglobin 7.0 16.7 Does all proteins separated properly w/ 2D gel electrophoresis?
- Complete the table below by adding (+) or (-) if eahc sample (amino acid or protein) below will test positive or negative, respectively. sample BIURET NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOSKIN-COLE G W H Y C R HAIR GELATIN CASEIN PEPTONE Identify the amino acid that will give the following data: BIURET NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOPSKIN-COLE - + + + - - + - Name of amino acid: structurte of the amino acid:Look at the amino acid composition of a protein given in the table and click on the area in the 2D gel electrophoresis where you may expect the corresponding band. Amino acid composition A D F G K L M P R V Y TOTAL: 16 2 12 14 9 2 9 1 7 3 11 3 2 11 11 10 1 3 164 Download Image.. pH7 pH 9 pH3 200,000 116,250 97,400 66,200 45,000 31,000 21,500 14,400 | ||| | |||Look at the amino acid composition of a protein given in the table and click on the area in the 2D gel electrophoresis where you may expect the corresponding band. Amino acid composition M N P 7 3 11 A D E F G K R S V W Y ТОTAL: 16 2 12 14 4 1 3 7 2 11 11 10 1 164 Download Image. pH7 pH 9 pH3 200,000 116,250 97,400 66,200 45,000 31,000 21,500 14,400 ||| | |||
- The A280 of a protein sample loaded onto a gel was determined to be 0.767 (1.00 cm path length, after subtracting the blank). The total volume of this sample was 428 µL. 19.0 µL of this protein sample was mixed with 19.0 µL of 2X laemalli sample buffer and then 12.0 µL of the entire sample was loaded into the gel and electrophoresed. Calculate the amount of protein that was loaded into the gel (in µg).A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol, three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein and clearly explain how you came to this determination.Using Bradford Assay, plot the standard curve and find the unknowns. Protein Concentration A595 of sample 0 0 3 0.220 6.5 0.383 12 0.667 18.8 0.930 24.2 1.090 Unknown 1 1.085 Unknown 2 0.708 Unknown 3 0.193