1. What is the function of each step or reagent used in the isolation of casein from milk? Reagents: a. Warm distilled water b. Vinegar c. Ethanol 2. What are the three general steps involved in the isolation of proteins? Discuss or briefly describe the purpose of each step. 3. Suggest a simple procedure (or test) to verify if the final product you obtained is indeed casein.
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1. What is the function of each step or reagent used in the isolation of casein from milk?
Reagents:
a. Warm distilled water
b. Vinegar
c. Ethanol
2. What are the three general steps involved in the isolation of proteins? Discuss or briefly describe the purpose of each step.
3. Suggest a simple procedure (or test) to verify if the final product you obtained is indeed casein.
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- We need to prepare a stock solution of medium for your culture cells, which usually includes liquid salt solution and bovine serum. Our liquid salt solution is supplied in a 50X concentration, and we need to dilute it to 1X for use. We also need to add 75% fetal bovine serum for a final concentration of 15%. How would we make up 0.80 liters of this culture media using water as our solvent?1. How do you determine the concentration and dilution of a solution using the tube dilution method? 2. Decide on what to do with this scenario. You are required to measure 1 mL of serum to be added to 5 mL reagent in a clinical chemistry assay. However, the amount of specimen that is left for you to work with is only 0.5 mL. What will you do if you are not allowed to take another specimen from the patient anymore?2. What are the possible problems or limitations of the standard plating techniques when used for the examination of hamburgers?
- 1. What are the sources, structural descriptions, and biological functions of gelatin, casein, and albumin? 2. Draw the respective chemical reaction involved in Xanthoproteic test, Millon’s test, Sakaguchi test, Hopkin’s-Cole test, and Sulfur test.4.outline the processes used in the preparation of agarose gel of 1.5 concentration 5.outline the procedures /steps in gel electrophoresis 6.how do we prepare x1(concentration) TAE buffer from 50x TAE buffer1: Complete the table below by adding (+) or (–) if each of the sample (amino acid or protein) below will test positive or negative, respectively.
- 1. Differentiate Precipitation from Agglutination reactions based on: a. Time duration of the procedure. b. Reactants involved. 2. Differentiate the following agglutination reactions based on the nature of a.) reagents used , and b.) unknown: a. Direct agglutination b. Passive agglutination c. Reverse passive agglutination d. CoagglutinationWhat will happen if the protein that you are assaying using zymography is not fixed properly using Trichloroacetic acid, and which step of the zymography is crucial for obtaining clear white bands on a bluebackground?Write down a detailed description about the formation of polyacrylamide gel, how it is used for protein separations and the process of electrophoresis in these gels.
- 1. What is the most common sterilization technique used in laboratories? 2. List at least 5 procedures of the aseptic technique and describe its uses. 3. Why is Gram stain one of the most important and widely used stains in bacteriology? 4. Explain the Gram staining technique in chronological order. Indicate the reagent used and the time of usage on each reagent.1. a 1 mL stock sample is added to 9 mL Of diluent to make solution A, and then 2 mL of solution A is added to 18 mL of diluent to make solution B. what is the final dilution with respect to the stock? 2. in most probably number (MPN) testing what media is used for confirming test and what does a positive result looks like? 3. In Most probably number (MPN) testing what can be inferred from a positive result on the presumtive test?I hope you can help me with this. When developing the zymogram using a destaining solution, a researcher observed wedge shaped bands with protein. What could be the possible reasons for such an observation?