Assume you have an SAR of 0.206 for sample 1; 0.271 for sample 2; and 0.606 for sample 3, what does this indicate? A larger increase in the purity of phycocyanin is seen after the use of ammonium sulphate, which removes other proteins A larger increase in the purity of phycocyanin is seen after the use of polyethylenimine, which removes other proteins A larger increase in the purity of phycocyanin is seen after the use of polyethylenimine, which removes nucleotides A larger increase in the purity of phycocyanin is seen after the use of ammonium sulphate, which removes nucleotides

Assume you have an SAR of 0.206 for sample 1; 0.271 for sample 2; and 0.606 for sample 3, what does this indicate? A larger increase in the purity of phycocyanin is seen after the use of ammonium sulphate, which removes other proteins A larger increase in the purity of phycocyanin is seen after the use of polyethylenimine, which removes other proteins A larger increase in the purity of phycocyanin is seen after the use of polyethylenimine, which removes nucleotides A larger increase in the purity of phycocyanin is seen after the use of ammonium sulphate, which removes nucleotides

Curren'S Math For Meds: Dosages & Sol

11th Edition

ISBN:9781305143531

Author:CURREN

Publisher:CURREN

Chapter5: Unit, Percentage, Milliequivalent, Ratio, And Household Measures

Section: Chapter Questions

Problem 2.8P

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A protein sample of unknown concentration was placed in a cuvette with a path length of 1 cm and the sample was found to have an A280 value of 2.92. If the protein of interest has an extinction coefficient of 44240 M-1 cm-1 and the molecular weight of the protein is 47.411 kDa, what is the concentration of protein in mg/mL?
Two proteins of different molecular weight (mw) are mixed and need to be separated. When eluted through a Sephadex-G50 chromatography column, what is the order of elution (first followed by second)? A. protein with mw of 40 kDa; protein with mw of 20 kDa B. both proteins will elute at the same time C. both proteins will not elute as the combined mw is larger than 50 kDa D. protein with mw of 20 kDa; protein with mw of 40 kD
Answer D E and F d) in base pairing, why do we never see AG, GA, CT or TC forming complementary base pairs? e) why is vegetarianism a more energy intensive process (from the organism standpoint) than being omnivores? [DON'T EVEN THINK OF STATING ANYTHING ABOUT FIBER, BULK, AND/OR CELULOSE!!!!] f) why is significant serum (in the bloodstream) cholesterol reduction so difficult, and why do most of the drugs designed to reduce cholesterol target the liver?
A mixture of proteins having molecular weights of 50 to 200 kDa can be fractionated linearly using a GFC column with an exclusion limit of at least _____.a. 25 kDab. 50 kDac. 125 kDad. 200 kDapls explain why
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PLEASE ANSWER ALL d) in base pairing, why do we never see AG, GA, CT or TC forming complementary base pairs? e) why is vegetarianism a more energy intensive process (from the organism standpoint) than being omnivores? [DON'T EVEN THINK OF STATING ANYTHING ABOUT FIBER, BULK, AND/OR CELULOSE!!!!] f) why is significant serum (in the bloodstream) cholesterol reduction so difficult, and why do most of the drugs designed to reduce cholesterol target the liver?
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For each of the following denaturing agents, explain the changes that you observed when each of them is added to an egg white in terms of change in protein structure at the molecular level. 1. heat 2. salt 3. baking soda 4. lemon juice 5. ethyl alcohol
What is the melting temperature and G/C content of the following primers? a.) 5’ GAAATAATTTTGTTTAACTTTAAG 3’ b.) 5’ GTAACTCAGCTTTCAGGTCG 3’
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After staining an SDS-PAGE gel with Coomassie Blue G-250, the protein bands are visualized by de-staining the gel in a Coomassie Blue G-250 de-staining solution. This solution is made up of 10% acetic acid, 50% methanol, and 40% distilled water. How much of each of these components do you need to prepare 5 liters of Coomassie Blue G-250 de-staining solution?
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