What is the Resource-Based Theory viewpoint of Strategic Human Resource Management & Human Captial?

Would the glucose test be suitable for analyzing the following samples? Which of the three unknown enzyme treatments would give positive results? Explain your answers.

• the amount of glucose present in a fruit
• the amount of carbohydrates in a beverage sweetened with high fructose corn syrup
• the number of monosaccharides present in a bacterial sample

In preparing protein sample for crystal structure : (a) Why is it necessary to use large amount of crystallisation solutions for the vapour diffusion experiment ? (b) Give reason why sitting drop format may be used for the experiment .(c) Explain why it will not be necessary to make selenium derivatives of enzyme used for the crystal trials .

BIOCHEM LAB: You measured the total protein in a sample of purified protein via the Bradford technique and find you have purified 1,000 mg in 1,000 ml total volume. You also measured the activity of this protein and found it to be 301 U. What is the specific activity (in U/mg) for this enzyme?

Many potent toxins and lethal poisons exert their effects by interfering with energy production in the cell. Select any such molecule (that interferes with energy production), and discuss which metabolic pathway it affects, particularly which enzyme(s) and how. -----> PLEASE TYPE 250 WORDS & INCLUDE 1 - 2 SOURCES, NO DIAGRAMS

1. This procedure recommends preparing E coli as spheroplasts to expose the alkaline phosphatase. Why is this a preferred strategy than simply completely lysing the bacteria completely?

2. Explain the unit 'Unit' when attempting to express a quantity of enzyme. Relate your definiton to the reaction taking place in the PNPP reaction.

Procedure A: A piece of fresh liver and little bit of water was put inside of test tube. The test tube was put inside of boiling water for five minutes. Test tube was taken out from boiling water and drained out the water. 2 mL of hydrogen peroxide was put inside of the test tube and only little bubbles (enzyme activity ) were formed.

Q1. What was the purpose of the assay performed?

Q2. Did increasing the temperature (heating the test tube) have an effect on enzyme activity? Briefly explain why.

Procedure B: 2mL of hydrogen peroxide was added to test tube. A piece of liver soaking in base/ alkaline solution was also put inside of test tube. Slowly, there are bubbles forming in almost to the top.

Q3. Under what pH condition is catalase most active? least active? Explain your answer using data from this part of the experiment.

A) You would like to sequence the genome of this organism. The restriction enzyme cut site for BglII is AGATCT. You will use it to clone fragments of the genome in order to sequence it. How many times would you expect this enzyme to cut within the chromosome of Andrebacillus wieczorius ? (2)

B) You decide to use a modified bacteriophage vector that can accommodate fragments digested with BglII. You use a partial digest on the chromosomal DNA. What are two reasons discussed in class that you need to use a partial digest in order to achieve your overall goal? (2)

C) Astonishingly, this is the first bacterium identified to generate a polyA tail on its transcripts! Wow! Considering that only 4% of the organisms’ genome codes for proteins, briefly describe how you would build a library of only the fractions of the genome that are rich in ORFs. In your answer, describe what type of a library this is called, the name of the technique,

An experimenter performs two sets of enzyme kinetics experiments. One set of experiments, when plotted as a double-reciprocal plot, yielded a y-intercept of 0.043 μM-1·min and an x-intercept of -20.0 mM-1. A second set of experiments, when similarly plotted, yielded a y-intercept of 0.129 μM-1·min and an x-intercept of -60.0 mM-1. The second set of experiments contained 92 nM of an uncompetitive inhibitor. Given these data, what is the Ki' (in nM to the nearest tenths) for this inhibitor? Hint: If you do not recall what the x-intercept represents, you can write the double-reciprocal equation and set 1/v equal to zero. Also, for this problem, you can assume that the enzyme exhibits Michaelis-Menten kinetics and that the estimates for Vmaxand Km that are obtained from a Lineweaver-Burke (i.e., double-reciprocal) plot are satisfactory. (Recall that I advocated in class for the use of nonlinear fitting algorithms.)