A 28-year-old female is hospitalized after being kicked in the left kidney during a soccer game. She is admitted to the critical care unit for observation. The nurse knows that one of the most important assessments of kidney and fluid status is the patient’s weight. In the critical care unit, weight is monitored __________. a. As needed b. Once per shift c. Daily d. Weekly The patient starts to deteriorate and the practitioner wants to accurately measure the patient’s body fluid status. Which of these values can be used to accurately assess the fluid volume status? (choose all that apply) a. Central venous pressure b. Intracranial pressure c. Pulmonary artery occlusion pressure d. Cardiac index e. Pulse oximetry f. Mean arterial pressure Diagnostic Procedures The practitioner also orders some lab work to be collected on the patient. One of the tests ordered is a serum creatinine. What is creatinine? a. A byproduct of protein and amino acid metabolism b. A byproduct of muscle and normal cell metabolism c. The concentration or dilution of vascular fluid and measures the dissolved particles in the serum d. Measures how well the kidneys remove creatinine in the urine One of the other labs the practitioner orders is a blood urea nitrogen

For each question, please explain how you got the answer.

1. The major function of RNA polymerase's sigma factor is
A) recognition of the translational stop sequence
B) recognition of the transcriptional start sequence
C) recognition of the transcriptional stop sequence
D) recognition of the translational start sequence
E) None of these are correct

2. WHere is the amino acid attached to a tRNA molecule?

A) 3′-hydroxyl of an adenine containing residue of 3’ end of tRNA
B) 5′-hydroxyl of a uridine containing residue of 3’ end of tRNA
C) 5′-hydroxyl of a guanine containing residue of 3’ end of tRNA
D) 3′-hydroxyl of a cytosine containing residue of 3’ end of tRNA
E) 2′-hydroxyl of a guanine containing residue of 3’ end of tRNA

3. Functions of RNA polymerase in E. Coli include
A) searching for promoter sites.
B) unwinding short stretches of DNA.
C) detecting termination signals.
D) searching for promoter sites and detecting termination signals.
E) All the answers are correct.

4. Actinomycin D inhibits transcription by:
A) binding to the DNA template by intercalation
B) binding to the RNA polymerase
C) binding to rho protein
D) Binding to the sigma subunit
E) none of the above

Answer all please

38. Which of the following inhibits the release of aldosterone?

a. low potassium

b. ACTH( adrenocorticotropic hormone)

c. Angiotensin 2

d. ANP( atrial natriuretic peptide)

12. which of the following substances CAN NOT be absorbed by the digestive system?

a. amino acid

b. triglyceride

c. monosaccgaride

d. Na+

0. growth hormone is anabolic for muscle and bone

a. true

b. false

40. which of the following is the correct function of PARATHYROID HORMONE?

a. increases blood calcium

b.increases blood phosphate

c. increases protein synthesis

d. ALL of the above

22. Lactose intolerance causes bloating and flatulence due to the absence of lactose dehydrogenase. Lactose is then consumed by microorganisms. The flatulence is generated by which portion of the digestive system?

a. stomach

b. small intenstine

c. Pancreas

d. Liver

E. Large intestine

36. The Adrenal Cortex secretes;

a. aldosterone

b. cortisol

c. DHEA(androgens)

d. all of the above

4. The peritoneum is:

a. a serous membrane surrounding and protecting abdominal organs

b. a connective tissue ligament attaching the liver to the stomach

c. the adventitia surrounding and protecting pancreas, duodenum and esophagus

d. an adipose layer storing nutrients for the abdominal organs

Biochemical Tests crossword puzzle:

Across

5 Anaerobic metabolism
6 Crusty growth on broth
8 Cloudy growth in broth
10 Smooth growth on slant
11 Another name for glucose
13 Hydrolyzed collagen
15 Possible sole carbon source
16 Bacterial movement
17 Test use of milk nutrients (2wds)
20 Hydrolyzes starch
22 Bacteria settled to bottom of broth
23 Milk sugar
27 Test for acetoin
28 Produces clear zones in skim milk agar
29 pH indicator in sugar fermentation tubes (2wds)

Down

1 Produced from tryptophan 2 Group of 4 tests
3 Red when acidic (2wds)
4 Turns SIM black
7 Catalysts secreted by the cell
9 Inverted tube to trap gas
12 Tests for lipase
14 Common liquid medium (2wds)
16 Sticky surface growth on broth
18 Breaking macromolecules with addition of water 19 Snowy appearance in broth culture
21 E. coli produces this from glucose (3wds)
24 Spiky growth on slant
25 Breaks down hydrogen peroxide
26 Product of amino acid degradation

1)     What is the main activity of the colon?

1. Reabsorbing water from the guts into the circulatory system

2. Absorbing water from the circulatory system to excrete from the body

3. Absorbing cellulose and glucose into the circulatory system

4. Absorbing amino acids and cellulose into the circulatory system

5. Killing off bacteria on the digested food

2)     Which of the following is important in inflammation?

1. Contraction of actin, myosin, and thrombosthenin

2. Increased permeability of capillaries

3. Activation of platelets

4. Antibody activation

5. Superoxide and hydrogen peroxide

3)     When oxygen-rich blood passes through a capillary bed in poorly-oxygenated tissue, what happens?

1. Hemoglobin delivers carbon dioxide to the tissue and picks up oxygen waste

2. Hemoglobin changes shape and much of the oxygen unbinds from the hemoglobin

3. Hemoglobin leaves the capillary and enters the tissue to deliver oxygen

4. Hemoglobin enters the capillary to carry carbon dioxide away from the tissue

5. Hemoglobin changes shape and most of the carbon dioxide unbinds from the hemoglobin

4)     If a person with type-O blood (the host) receives blood from a type-A donor, what are the consequences?

1. There is no clotting because there are no antigens on the donor’s type-A blood

2. Both A and B are true

3. The type-A donor blood clots because of the anti-B antibodies in the host’s body

4. The type-A donor blood clots because of the anti-A antibodies in the host’s body

5. There is no clotting because there are no antibodies in the host’s type-O blood

5)     Which of the following statements best explains how the amount of water inside alveoli remains small?

1. The lymphatic system drains fluids from the alveoli

2. There are large amounts of proteins in the water inside the alveoli, which dilutes the water

3. There are large amounts of proteins in the interstitium, causing water to leave alveoli via osmosis

4. The fluid in the alveoli is passed into the esophagus

5. The question is wrong; the alveoli have large amounts of water in them

6)     Which of the following statements about hydrochloric acid in the stomach is FALSE?

1. Begins the process of breaking down fats

2. Kills many pathogens that enter the stomach

3. It is responsible for activating pepsinogen into pepsin

4. Its production results in an increase in bicarbonate in the blood

5. Denatures proteins in the stomach

7)     A protein designed to attach to one kind of invading structure (protein, carbohydrate, or other structure or chemical that identifies the invader) is:

1. Lymphocyte

2. Rh factor

3. Antibody

4. Antigen

5. Lysosome

8)     Which of the following statements about T-lymphocytes is true?

1. They are responsible for manufacturing antibodies

2. Some kinds of T-lymphocytes bind to invaders, puncture them, and poison them

3. They are manufactured in the bone marrow

4. Each T-lymphocyte can react to dozens of different antigens

5. They are related to humoral immunity, and not cell-mediated immunity

9)     When an action potential is inhibited, which of the following statements describes the voltage change?

1. Neurotransmitters are not produced in adequate amounts to carry on an action potential

2. Sodium ions are drawn into the axon and not released

3. Too much neurotransmitter is produced, causing the action potential to damage the axon

4. A greater voltage change is required because the resting voltage is unusually negative

5. A smaller voltage change is required because the resting voltage is close to zero

10)   Which of the following type of white blood cells (leukocytes) moves via amoeboid locomotion?

1. Erythrocytes

2. Lymphocyte

3. Basophils

4. Platelets

5. Macrophages

11)   When a person sees a car driving on the road, and simultaneously hears the motor, the two sensory inputs can be combined to form a more complete understanding of the situation. This is an example of:

1. Afferent and efferent interaction

2. Chemosensitivity

3. Partial pressure

4. Integrative function

5. Facilitation

12)   During exercise, the blood flow to the lungs increases by:

1. Decreased pressure in the pulmonary arteries

2. Greater pressure from the left ventricle of the heart

3. Greater number of open capillaries

4. More rapid contractions of the diaphragm

5. Slow, strong contraction of the diaphragm

Imagine that you’ve cloned something that you think is a cadherin, but you know very little about it (and hopefully nobody knows anything about it, otherwise it wouldn’t be “research”). You think it is attached to the cytoskeleton, hypothetically through its cytoplasmic tail. Your goal is to identify the part(s) of the cytoplasmic tail that is/are responsible for binding. Luckily, if you’ve cloned a gene, it is easy to make sub-clones that have specific portions of the polypeptide strand deleted. This is usually denoted by “delta” (ΔCx would be missing region #x of the cytoplasmic tail).

To achieve this goal, you would use a technique called immunoprecipitation, followed by SDS-PAGE (western blotting). The new part is immunoprecipitation, but do not worry; below the problem setup is a video for more info on this technique – which is like an add-on to the beginning parts of the SDS-PAGE/western procedure that you are already familiar with.

Basically, you use an antibody that binds to your cadherin (you can design an antibody for it, once you know the DNA sequence from the cloning step) to “pull down” your cadherin. Anything directly attached to your cadherin though, will also get pulled down with your antibody. Then you can throw away all of the other cell components – next you release the proteins from the antibody and make a liquid out of this “precipitated protein” that you pulled down – and finally you load the liquid on an SDS-PAGE gel just as we did with the “total protein” from the cytoplasm of the yeast cells. The difference (compared to what we did in lab) is that if we now use another antibody (like anti-GFP) at the end of the procedure to find the detectable proteins in our experimental system – only other proteins that were pulled down with the cadherin could possibly show up, not just any-and-all proteins that contain GFP that were in the cell lysate (liquid cell mash). Assume that we have GFP tags and antibody labelling abilities, for all candidate binding partners of the cadherin.

From the results, you can see that three proteins pull down. An approximately 110 kilodalton (kDa), a 97 kDa, and an 80 kDa protein all seem to bind with our cadherin (based on the “intact” experiment on the left; with cells that express the normal cadherin that can bind to everything that it normally wants to bind). Answer the questions below regarding the other experiments. Use panel (B) to understand what is in the lanes (the thin parts are the regions deleted, TM means “transmembrane”, the numbers are not relevant but they correspond to the number of amino acids that are deleted).

Linear Diagram of

our Cadherin

1. Which region (give a number 6, 7, 8, 9 or 10) is responsible for binding to the 97 kDa partner of the cadherin?

2. How do you explain the fact that deleting region #6 abolishes all three binding interactions? Think of protein structure/function from the in-person classes as well as the ECM lecture about cadherins (what would be the role of the transmembrane region in the overall protein structure and its ability to bind to partners).

3. Explain how the results from mutant ΔC9 (in which all three binding sites are deleted) is different than the explanation in part ii. In other words, where does the 110 kDa protein bind, and where does the 80 kDa protein bind on the cadherin? How do you explain the results from lanes 2 and 5 being the same, even though the experiments were different?

4. mOsT EXtreme ScIEntIfIc cHaLLeNge: How do you explain the results in lane 6, which seem to suggest that mutant ΔC10 still has binding to the 97 kDa partner – even though mutant ΔC10 is missing regions 7, 8, 9, and 10? Again, think of protein structure/function – and be creative.

Economic laws have been true throughout human history. As an example, consider the following passage, from Professor Samaddar’s lectures on the economy of Ancient India:

“Weaving in India has been encouraged from time immemorial... As is the case now-a-days, labourers working overtime were given extra payment... and special rewards were given for working on holidays.” (p.117)

Using a supply and demand diagram in the market for labour, clearly explain why Indian workers working overtime or during holidays were paid extra

Biodiversity loss is one of the more important environmental issues humans need to address. a. (3 pts.) Name two ecosystem services biodiversity provides and why each is important. b. (3 pts.) Name three human activities that are threats to biodiversity? Which is the greatest threat and why? c. (2 pts.) What can society and individuals do to reduce the risk of extinction (list at least two things). Name a MN threatened/endangered species we talked about that would be helped by these actions.