most amount of attraction to an anion column operating at the physiological ph
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based on the chart answer the following question
1. which protein will have the most amount of attraction to an anion column operating at the physiological ph
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- asapDescribe the biochemical role of coenzyme Q10 and how supplementation may impact metabolism. Be sure to address the key terms listed below as part of your discussion; you may address additional etiologies as well. coenzyme Q Complex I Complex II Complex III ubiquinone ubiquinol Electron transport chain Oxidative phosphorylation Reactive oxygen speciesThe table below shows the purification of liver lactate dehydrogenase. Purification Table of liver LDH Step Crude Extract Ammonium Sulfate DEAE-Sephadex 5'AMP-Sepharose Volume (mL) 200 100 112 40 LDH activity (Units/mL) (mg/mL) [Protein] 47.0 50.00 90.0 63.00 51.0 1.50 137.0/ 0.4 Calculate the LDH yield for the ammonium sulfate step. Provide answer to one decimal only. Show Transcribed Text this is biochemistry and the topic is protein purification could you pleaae show me the full workings even the workings for the comversions
- Consider the proteins in the table below. Protein Isoelectric point (pl) М.W. Alcohol dehydrogenase 150,000 5.5 Cytochrome C 12,400 10.5 Serum albumin 66,000 5.3 B-Amylase 200,000 5.7 Apoferitin 443,000 4.0 Fill in the blank. If the mixture of proteins above was subjected to anion exchange chromatography at pH 8, from the column. would be the first protein to elutedraw acyl coa derived from docosanoic acid C21H43CO2HOptimum temp of amylase was identified by incubation of the amylase together with starch at various temps for 10 mins. and stopped with HCI. The volume of added DNS is negligle. Volume Volume Volume Concentration of Temperature (°C) of of stock of stock starch distilled Absorbance amylase starch (mg/mL) water (uL) (mL) (mL) 1 1 10 9 0.0053 10 1 1 10 9 0.1309 20 1 1 10 9 0.1185 30 1 1 10 9 0.0531 40 1 1 10 0.0206 Using this graphically determine the optimum temp of amylase?
- You have a crude lysate sample (CL) containing a mixture of six proteins (1, 2, 3, 4, 5, ẞ- galactosidase), and your goal is to obtain purified ẞ-gal. Some characteristics of these proteins are shown in the table below. Protein Alcohol dehydrogenase Carbonic anhydrase Insulin B chain Phosphorylase B Glutamic dehydrogenase B-galactosidase 45% Concentration of ammonium sulfate (AS) required for precipitation Molecular Weight (kDa) Isoelectric point (pl) 38 3.7 80% 65% 20% 30% 45% 28 4.8 4 5.3 98 6.8 49 9.5 115 5.3 You begin your purification by performing an ammonium sulfate (AS) precipitation. You add the appropriate concentration of AS to your CL sample, incubate overnight at 4°C, then centrifuge to generate a supernatant (AS-S) and pellet (AS-P). What concentration of AS will you use to precipitate Glutamic dehydrogenase? © 20% O 30% 45% 65% 80%Handwritten Identify the molecule names, enzyme name, enzyme classification and change in reaction(for glycolysis pathway)Enzyme Triacylglycerol Lipase Rennin Catalase Hexokinase Enzyme Official Name (write N/A if not applicable) Enzyme Official Number (4 digits) Simple or Conjugated Enzyme (specify cofactor if applicable) Type of Reaction Catalyzed Substrate Optimum pH Optimum Temperature Function/s Disease (give 1 and describe briefly)
- Glutamate is derived from which of the following molecules? oxaloacetate pyruvate O 3-phosphoglycerate chorismate O a-ketoglutarateFor myristic acid, C 13H 27CO 2H: (a) How many molecules of acetyl CoA are formed from complete β-oxidation? (b) How many cycles of β-oxidation are needed for complete oxidation?What is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1