1.Name the enzyme(s) that is defected in methionine metabolism
2 .Define” fast” and “Slow” protein
3. What is the difference in absorption and metabolism of Fast and Slow protein?
4.Explain what happen to protein during the postabsorptive phase, discuss the hormones involved and their role and relations in protein synthesis
5. Mary is a 25 years old postoperative patient at the health clinic on campus. With an 80gm protein intake, and a 10-gram urea nitrogen output. Please calculate Mary’s nitrogen balance status. Is she in positive, negative, or at equilibrium? Based on her nitrogen status, explain what could be the possible reason for her nitrogen status
In: Nursing
A accidental genetic mutation in the lab mice has occurred and affects the glycogen degradation pathway. Dr. Wilson is studying this unexpected mutation and has taken samples of their livers. What he found was excessive glycogen storage but the glycogen structure was unusual. There was a lot of glycogen but size of each glycogen molecule was smaller and each chain end had 4 glucose units (alpha 1,4 bonds) and then a SINGLE glucose attached as a branch point (alpha 1,6 bond) to the 5th carbon from the end. Which enzyme in the glycogen degradation pathway is not working?
| phosphoglucomutase |
| glycogen phosphorylase |
| glycogen transferase |
| alpha-1,6-glucosidase |
| glucose 6-phosphatase |
In: Chemistry
As a new targeted anti-cancer drug ‘FCIC-17’ enters Phase III clinical trials, it is determined that the drug requires hepatic activation in order to elicit a therapeutic effect. Further studies identify that the sole enzyme involved in the activation of this drug is CYP2C19.
Questions:
a) Select ONE specific factor (from the categories environmental, genetic or physiological) that may contribute to inter-individual variability in the activation of ‘FCIC-17’, and explain the potential consequences of this variability in terms of treatment response and tolerability. (250 words; 5 marks)
b) Briefly discuss how this variability may be controlled for in clinical practice. (150 words; 3 mark)
In: Biology
BioChemistry Lab question:
Your PI would like to measure the concentration of alanine aminotransferase (ALT), a liver enzyme, in a homogenate of mouse liver. Your lab already has a bottle of ALT and a very specific and selective antibody that is known to bind to ALT and ALT only. What technique will you use to measure ALT in the liver homogenate? Why choose this/these technique/s? Briefly describe the results you would obtain from each technique.
This is a lab question and so far in the class, we have done immunoblot, electroblotting, ELISA, Bradford Coomassie assay, protein ladder, SDS-PAGE, and Column chromatography.
In: Biology
This flowsheet is from the MIT OpenCourseware website, “Separation Processes for Biochemical Products”, taught in 2005. It shows the downstream steps for recovery of alkaline protease, a biological enzyme. You can view these interesting lecture notes at http://ocw.mit.edu/courses/chemical-engineering/10-445-separationprocesses- for-biochemical-products-summer-2005/lecture-notes/lecture_10.pdf after the midterm (they tie in nicely with 4N4 also).
1. What is the general purpose of flocculation?

2. What is the purpose of flocculation in this flowsheet?
3. What is the purpose of the membrane step here?
4. Why are these membrane units in series?
5. Is it the retentate or permeate that is of interest?
In: Chemistry
you notice that a particular eukaryotic mRNA fails to undergo the process of capping. You, as a scientist come pu with multiple ways to help out this mRNA function. Out of al the methods there was one which was incorrect. Which one out of all your expt would not work...? A) you try to attach a compound to the MRNA that would get it out of the nucleus B) you try to stall the mRNA in the nucelus until the cell machinery can eventually start synthesizing a cap C) you try to increase the dose of the enzyme poly A polymerase D) you try to increase the levels of proteins that inhibit the function of exunucleases
In: Biology
In: Biology
Two charged proteins P1 and P2 are located at positions (1m,1m) and (-1m,1m) respectively on a Cartesian coordinate system. They have charges of 1.0 nC and -1.0 nV respectively. A key enzyme E1 which regulates an important biochemical pathway, is localed at the origin of the coordinate system.
In: Physics
4. The following table presents the data on comparison of three methods of determining serum amylase values in patients with pancreatitis. Test whether these data indicate a difference among the three methods.
|
Serum amylase values (enzyme units per 100 ml of serum) in patients with pancreatitis |
|||
|
Specimen |
Method of determination |
||
|
A |
B |
C |
|
|
1 |
4000 |
3210 |
6120 |
|
2 |
1600 |
1040 |
2410 |
|
3 |
1600 |
647 |
2210 |
|
4 |
1200 |
570 |
2060 |
|
5 |
840 |
445 |
1400 |
|
6 |
352 |
156 |
249 |
|
7 |
224 |
155 |
224 |
|
8 |
200 |
99 |
208 |
|
9 |
184 |
70 |
227 |
In: Statistics and Probability
Your company, DrugsRUs, has developed a generic angiotensin-converting-enzyme inhibitor, Vasotec, as a pharmaceutical drug used primarily for the treatment of hypertension and congestive heart failure. You are leading the regulatory strategy team and have been asked to describe the path to approval comparing introduction in the US versus Brasil.
Please discuss the following:
(1) Which agency or agencies will be responsible for approving/reviewing your Vastec drug: (a) before commercial introduction, and (b) after approval for commercialization/sale within the US., and
(2) Compare known issues your company will need to consider to market your generic drug is Brasil.
In: Biology