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Tuna Composition Assignment Help Available

Tuna Composition
Tuna Composition

Tuna Composition Research Paper

Tuna Composition

– Background information about the type and source of Tuna, including composition information.
– How to sample the Tuna and how to storage Tuna after sampling.
– Laboratory management including a HIRAC report for each analysis. (hazardous and dangerous chemicals).
– Timeline for completion of the analysis and the quantity of sample required for each test.

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Phosphoglycerate mutase Enzyme

Phosphoglycerate mutase Enzyme
Phosphoglycerate mutase Enzyme

Phosphoglycerate mutase Enzyme

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ENZYME: Phosphoglycerate mutase

The purpose of this assignment is to encourage you to integrate lecture material on protein structure and enzyme function, with the biochemical and biological role of a key metabolic enzyme. The listed proteins have been chosen because they play an important role in carbohydrate metabolism.

You must research the following information about your protein:

Structure: is it a globular, membrane or structural protein; include a figure showing a molecular model of your protein; describe its structure including secondary structures, any domains, quaternary structure, any prosthetic groups; include the molecular weight and isoelectric point of your protein.

Function: Write an equation for the reaction catalysed by your enzyme; in what pathway does your enzyme participate. In what organisms, organs, tissues, cells, intracellular compartment is the enzyme and pathway found? What is the metabolic purpose of the pathway? What is the importance of your enzyme in that pathway (e.g. regulation, thermodynamics)? Relate the biochemical function of your enzyme to practical information such as clinical data.

Relationship between structure and function: describe any features which are particularly important for catalytic function such as specific amino acids with a key function, the 3 dimensional structure of the active site or binding site. Is your enzyme soluble or membrane protein and how does this relate to its function? What role is played by any co-factors? Is your enzyme regulated? Describe any changes to structure that occur during regulation explaining how the structure affects enzyme activity.

Pitfalls to avoid:

Choose ONE organism as your main focus; the enzymes in the list are found in many different organisms but there will often be major differences between enzymes in humans and E. coli.Sometimes information on one organism may be limited so it may be necessary to have a figure of e.g. a pig enzyme if you are mainly discussing the human version; mixing up info on human and yeast will result in loss of marks.
Be aware that some enzymes are present in several isoforms, do not get these confused.

SAMPLE ANSWER

Question 1

Phophoglycerate mutase (PGM) is a globular protein common in glycolytic activities. The secondary structure is an alpha/beta protein with three main layers as comprising of an alpha/beta/alpha. Additionally, it has a beta sheet comprising of six strands arranged in a specific order with strand 5 occurring as an antiparallel to the rest of the strands. The quaternary structure is made of two identical subunits hence can be categorized as a homodimer. The realative molecular mass of dimers is 55,000 -61,000 kDa. The quaternary is same as the primary, secondary and tertiary structure on the basis of active sites.  However, the PGM is has isozymes, which is several variations existing. The type of an enzyme isozyme catalyzing a reaction depends on the tissue where the enzyme is active (Fraser, Kvaratskhelia & White, 1999).

There are two forms of the glycolytic phosphoglycerate mutase (PGM) which are evolutionary unrelated. They occur as non-homologous isofunctional(NISE), each with an independent 3D structure. The first is the co-factor dependent PGM (dPGM) works in the presence of the co-factor 2, 3-bisphosphoglycerate (2, 3-BPG). It has a molecular weight of 27 Kd, and are active as dimmers. The other type of the enzyme is the co-factor independent PGM (iPGM) has a molecular wight of 57 Kd. The enzyme is active in the monomer.

The distinction between the two forms of PGM can be determined by level of sensitivity to vanadate and metal ion requirement of iPGM. E.coli contains both iPGM and dPGM (Foster, 2010). Like the mammalian dPGMS, the E. coli dPGM forms a dimer which now enables researchers to analyze the sequence differences that are responsible for the variation in the quaternary structure.

The structure of the protein allows the function of the two enzyme domains to be assigned. One of the domains takes part in the phosphatase reaction, leading to the generation of the phosphoserine enzyme intermediate. The other domain participates in the phosphotransfterase reaction leading to reformation of the phosphoglycerate (Jedrzejas et al., (2000).

(EC 5.4.2.11 – Phosphoglycerate mutase, n.d)

Question 2

The enzyme phosphoglycerate mutase is involved in the glycolysis where it catalyzes the interconversion of 3-phosphoglycerate and 2-phosphoglycerate for zymomnas mobilis’ glyconeogenic and glycolytic pathways.  The phospho group is transferred between the three phosphoglycerate carbon atoms. The co-factor dependent PGM (d PGM) catalyzes the transfer of a phosphoryl group between the co-factor and the monophosphoglycerate via an intermediate, phosphohistine. It is important in the transfer of a phospho group between monophosphoglycerates via a phosphoserine intermediate. The respective function of both iPGM and dPGM has not been established. However, research has shown that dPGM accounted for more activities (Foster, 2010).

The relevance of PH sensitivity in physiological processes because plays a role in regulating the activity of iPGM at different stages of an organism’s developmental cycle. For instance, the PH of a developing spore drops to about 6.5 during sporulation which leads to the reduction in the iPGM’s activities. The low PH allows 3PGA to accumulate and is stored in the dormant spore. This 3PGA is used to synthesis ATP required in spore germination, again leading to a sharp rise in the PH to 7.5-8. In non-spore forming organisms that are closely related to those that reproduce by sporulation, iPGMs, Mn2+ is also required for catalysis.

The mechanism of iPGM catalysis of 2-phosphoglycerate occurs in two steps as this is a phosphatase reaction in which a phosphate group is transferred from 2 or 3-phosphoglycerate,forming an enzyme-bound phosphoserine intermediate, then a phosphotransferase reaction. Meanwhile, the phosphate is transferred from the enzyme-bound phospherine back to the glycerate moiety.

Reaction:  

2-phospho-D-glycerate = 3-phospho-D-glycerate.


2-phospho-D-glycerate		 =
3-phospho-D-glycerate

(EC 5.4.2.11 – Phosphoglycerate mutase, n.d)

The co-factor dependent PGM is capable of catalyzing three various reactions, each with its own type of specificity. The reactions include the synthesis in which 1,3-DPGforms  2,3-DPG where 3-PGA  is the primer, isomerisation reaction in which 3-phosphoglycerate (3-PGA) is formed from 2-phosphoglycerate (2-PGA) where the primer is 2,3-diphosphoglycerate (2,3-DPG) and degradation leading to formation of 3PGA from 2,3-DPG in a phosphatise activity. Also, the analysis of dPGM shows the enzyme ligand interaction which takes place to where the vanadates inhibit the mutase activity.

Phosphoglycerate mutases (PGMs) enzymes are important in glycolysis and gluconeogenesis reactions. In the glycolytic catalysis, 2-phosphoglycerate (2PG) is formed from 3-phosphoglycerate (3PG) through the intermediate 2, 3-bisphosphoglycerate. The reaction said to be energetically neutral since the Gibbs energy involved being approximately 1.1KJ/mol. The neutral state of the energy is absolutely necessary for the generation of the proper molecule required to continue the glycolysis process.

The reaction catalyzed by PGM

3PG + P-Enzyme → 2,3BPG + Enzyme → 2PG + P-Enzyme
3-phosphoglycerate -> intermediate -> 2-phosphoglycerate

Analyses of structure and sequence indicate that various families of the phosphatase enzymes contribute to different branches which are added to the parent enzyme. For example, histidine phosphatase superfamily is given this name because the catalytic reaction centres on the conserved on the His residue. This residue is transiently phosphorylated during the catalytic cycle. There are other conserved residues which interact with the phosphor group besides contributing to the “phosphate docket”.  Different residues are added to the “phosphate pocket”. The families which contribute the residues differ in the three dimensions, position and sequence of a catalytically essential residue acidic residue Bond, White & Hunter, 2002.).

Question 3

  1. coli’s structure of dPGM is complexed with vanadate, which is a potent inhibitor. The presence of the inhibitor in the active site although there is evidence indicating that there is additional vanadate moieties at both or either ends. The presence of the inhibitor also represents a different binding mode from the one observed on the structural homologue proctatic acid phosphatase. The analysis of dPGM reveals a water molecule in the native E.coli dPGM structure. Once this molecule is activated by vanadate, the active site protein is likely to be dephosphorylated. The binding of substrates as well as other specific interactions of both forms of dPGM’s active and inactive forms may be easily studied with a provision of the forms’ high-resolution structure in conjunction with computational substrate molecule modelling in the active site (Jedrzejas et al. 2000).

iPGM differs from thedPGM in that it only catalyses  out interconversion of  2PGA and 3PGA (1, 3, 4). The other difference is that catalysis by co-factor dependent phosphoglycerate mutase does not require metal ion while the iPGM absolutely or specifically require Mn 2+ ions hence making the enzyme’s activity exquisitely sensitive to PH (1, 4, 6-8). In clinical practice, a number of diagnostic procedures rely on the PH values   to determine the cause or level of infection (Jedrzejas et al. 2000).

Fig:. DS-PAGE analysis of purification and protein expression: Lane 1, size markers; lane 2, total soluble protein for cells expressing dPGM; lane 3, purified dPGM; lane 4, total soluble protein for cells expressing iPGM; lane 5, purified iPGM (Fraser, Kvaratskhelia & White, 1999).

The E. coli PGM is a protein hence is soluble in water although to different extents depending on the provided conditions. One of the conditions is the presence of Isopryl-1-thio-β-D- galactopyranoside. iPGM’s solubility impacts its ability to aggregate with other groups through chemical reactions. Solubility infers that the protein has negative charges. The solubility discriminates the reactions the enzyme can catalyze (Fraser, Kvaratskhelia & White, 1999). As mutase, PGM is an important step during glycolysis. The transfer of a functional group such as a phosphor group from one position of a substrate to another is catalyzed by the enzyme, hence the reaction becomes isomerisation. It will not function if it not subjected to the right conditions for solubility to occur.

The co-factor dependent phosphoglycerate mutase (dPGM) is found in a dimeric active conformation in Escherichia coli (E.coli). It is reactions are based on the structural changes which occur on the histidine phosphorylation exhibits a number of features which are fundamental in the catalytic mechanisms of the enzyme. During reactions, the C-terminal 10-residue tail which does not appear in other structures is ordered well so that to interact well with other residues involved in substrate binding. During the displacement of a loop positioned close to or adjacent to the active histidine leads to the readjustment of previously overlooked residues into positions which will make it easy for them to directly influence the catalysis (Bond, White & Hunter, 2002.).

References

Foster, J., Davis, P., Raverdy, S., Sibley, M., Raleigh, E., Kumar, S., … Ahmed, N. (2010). Evolution of Bacterial Phosphoglycerate Mutases: Non-Homologous Isofunctional Enzymes Undergoing Gene Losses, Gains and Lateral Transfers. PLoS ONE, E13576-E13576.

Jedrzejas et al., (2000). Mechanism of Catalysis of the Cofactor-independent Phosphoglycerate Mutase from Bacillus stearothermophilus. CRYSTAL STRUCTURE OF THE COMPLEX WITH 2-PHOSPHOGLYCERATE. Journal of Biological Chemistry, 23146-23153.

Bond, C., White, M., & Hunter, W. (2002.). Mechanistic implications for Escherichia coli cofactor-dependent phosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex. Journal of Molecular Biology, 1071-1081.

Fraser, H., Kvaratskhelia, M., & White, M. (1999). The two analogous phosphoglycerate mutases of Escherichia coli. FEBS Letters, 455(3)344-348.

EC 5.4.2.11 – Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). (n.d.). Retrieved November 19, 2014, from http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/enzymes/GetPage.pl?ec_number=5.4.2.11

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Eggs Protein foams Cheese Lab report

Eggs Protein foams Cheese Lab report
Eggs Protein foams Cheese Lab report

Eggs Protein foams Cheese Lab report

The report should be divided into the following sections:
1. Introduction – Should include a clear statement regarding the purpose of the experiment.

2. Methods – Refer to the experiment/procedure available on the NUTR 1102 Laboratory
Moodle sit

3. Results – Include data tables as completed in lab. Means and standard deviations should be calculated and correct. Tables and figures should be numbered and labelled and appear in the order that they are referred to in the text. The reader should be able to look at the table and understand its contents without reading the report.

4. Discussion – A discussion of the results and what they mean. This section will probably be longer than other sections of the report; however, be as concise as possible. Marks will be taken off for irrelevant information. It is not necessary to repeat information
provided in the tables. You will need to refer to the tables and graphs in the Results section. Be sure to specify which table or graph you are referring to, i.e. (Table 2) or (Figure 1), etc. Try to discuss in experimental blocks. Integrate objective and subjective data. In the discussion, try to explain why you got the results that you did, especially if they differed from the expected. Does literature support or negate findings? Was there something about the samples or testing environment that could have caused the deviation from the expected, i.e. fluctuations in oven temperature, personal element, untrained panel, sensory fatigue. Were any trends evident? Discussion should be supported with
theory and referenced accordingly. References should be listed numerically in the order they appear in the report. Numbers should appear in brackets following the citation. The full reference should be listed at the end of the report under the References section.

5. Conclusions – A brief summary of what the experiment has shown and possible implications or applications (food service, food industry, domestic, consumer retail level, etc.). This section should give the reader an idea of the purpose and usefulness of the tests without reading the rest of the lab report.

6. References – A list of only those references cited in the report should be included. Full references should be listed numerically in the order they appear in the report. In addition.

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Knowledge of Foundation Concepts

Knowledge of Foundation Concepts
Knowledge of Foundation Concepts

Knowledge of Foundation Concepts

Order Instructions:

Assignment Assess your Knowledge of Foundational Concepts
Assess your knowledge of foundational concepts essential to the nursing management of client health by taking the interactive quiz, located in the media “Arterial Blood Gas Interpretation.” http://lc.gcumedia.com/zwebassets/courseMaterialPages/nrs410v_self-assessment-v1.1.php
The quiz is designed as a tool for self-assessment. When you encounter questions that seem vaguely familiar, click on the media’s study materials, which are organized by topic (e.g., anatomy, biology, chemistry, pharmacology). This media will serve as a refresher for the concepts that build upon one another in nursing practice.
You will have the opportunity to retake the quiz until you achieve a passing score of 100%.
Once completed, please save your results and submit to the instructor.

SAMPLE ANSWERS

Knowledge of Foundation Concepts

Student ADA Version

of the Arterial Blood Gas Interpretation Pre-Assessment

Anatomy

Backward effects of left-sided heart failure include:

  1. Pulmonary congestion
  2. Jugular vein distention
  3. Dependent edema in the legs
  4. Bounding pulses

Anatomy

In performing a physical assessment, the nurse notes the patient has a “barrel” configuration to the chest. This is a consequence of:

  1. Reduced intrapleural pressures
  2. Bronchial airway expansion
  3. Increased vital capacity
  4. Increased residual lung volume

Student ADA Version

of the Arterial Blood Gas Interpretation Pre-Assessment

Anatomy

Backward effects of left-sided heart failure include:

  1. Pulmonary congestion
  2. Jugular vein distention
  3. Dependent edema in the legs
  4. Bounding pulses

Anatomy

In performing a physical assessment, the nurse notes the patient has a “barrel” configuration to the chest. This is a consequence of:

  1. Reduced intrapleural pressures
  2. Bronchial airway expansion
  3. Increased vital capacity
  4. Increased residual lung volume

 

Anatomy

Ausculation of the chest reveals bilateral fine crackles in the bases bilaterally, indicating:

  1. Right-sided heart failure
  2. Left-sided heart failure
  3. Pneumonia
  4. Acute respiratory distress syndrome

Biology
The signs and symptoms of anemia are all related to what common pathophysiologic feature of the condition?

  1. Increased oxygen consumption by tissues
  2. Decreased blood oxygen content
  3. Vasodilation
  4. A shift in the oxyhemoglobin dissociation curve

Biology
In addition to hypertension, preeclampsia is characterized by:

  1. Nausea and vomiting
  2. Fatigue and lower back pain
  3. Protein in the urine and edema
  4. Retinal changes and rates in the lungs

Biology
Common manifestations of bacterial pneumonia include all of the following except:

  1. Fever
  2. Productive Cough
  3. Tachypnea
  4. Hyperinflation

Biology
Closed drainage systems work to re-expand a lung after pneumothorax by:

  1. Re-establishing the normal negative intrapleural pressure.
  2. Creating a positive pressure in the pleural space
  3. Removing excess fluid from the pleural space so that there is room for lung expansion.
  4. Pulling oxygen into distal air sacs to re-expand lung tissue

Biology
Patients with chronic renal failure usually exhibit:

  1. Bradycardia
  2. Hypokalemia
  3. Hypocalcemia
  4. Hematomas

Biology
The diet of a patient in end-stage kidney disease is restricted in all of the following except:

  1. Fluid
  2. Potassium
  3. Protein
  4. Calories

Anatomy

Which of the following is true of the biological functions of progesterone?

  1. Progesterone is the most important hormone associated with pregnancy.
  2. Progesterone directs male sexual characteristics.
  3. Levels of progesterone increases if the egg is not fertilized.
  4. Levels of progesterone remain stable if the egg is not fertilized.

Anatomy

Which of the following is true of the biological functions of testosterone?

  1. Testosterone is not secreted by the ovaries.
  2. Testosterone is needed for development of female secondary sexual characteristics.
  3. Testosterone stimulates ovulation.
  4. Testosterone is needed for development of male secondary sexual characteristics.

Anatomy

Which of the following is true of the biological functions of estrone?

  1. Estrone is required for proper development of male secondary sexual characteristics.
  2. Level of estrogen degreases if the egg is not fertilized.
  3. Estrone is required for proper development of female secondary sexual characteristics.
  4. Estrone affects only the reproductive organs.

Biology

What is the function of hemoglobin?

  1. Hemoglobin is the protein in red blood cells that is responsible for carrying oxygen to the cells of the body.
  2. Hemoglobin is a lipid in red blood cells that is responsible for carrying oxygen to the cells of the body.
  3. Hemoglobin is a protein in white blood cells that is responsible for carrying oxygen to the cells of the body.
  4. Hemoglobin is a protein in red blood cells that is not responsible for carrying carbon dioxide to the cells of the body.

Biology

Why is heat an effective means of sterilization?

  1. Heat is an effective means of sterilization because it destroys the proteins of microbial lifeforms, including fungi, bacteria, and viruses.
  2. Heat is an effective means of sterilization because it destroys the proteins of anaerobic microbial lifeforms, including fungi, bacteria, and viruses.
  3. Heat is an effective means of sterilization because it destroys the lipids of microbial lifeforms, including fungi, bacteria, and viruses.
  4. Both (B) and (C).

Chemistry:

List the enzymes whose levels are elevated in the blood serum following an MI.

  1. CPK, LDH, AST, and SGOT
  2. LDH, AST, and SGOT
  3. CRE, AST, and ALT
  4. None of the above

Chemistry

What is the physiological function of gluconeogenesis?

  1. Gluconeogenesis is production of glucose from noncarbohydrate molecules in times when blood glucose levels are low. This ensures proper function of brain and red blood cells, which only use glucose as fuel.
  2. Gluconeogenesis is production of glucose from noncarbohydrate molecules in times when blood glucose levels are high. This ensures proper function of brain and white blood cells, which only use glucose as fuel.
  3. Gluconeogenesis is production of glucose from carbohydrate molecules in times when blood glucose levels are low. This ensures proper function of brain and red blood cells, which only use glucose as fuel.
  4. None of the above

Chemistry

What effect does glycogen metabolism have on glucose levels?

  1. Glycogen metabolism traps glucose within liver cells and increases storage of glucose in the form of glycogen. These processes decrease blood glucose levels.
  2. Glycogen metabolism traps glucose within liver cells and increases storage of glucose in the form of glycogen. These processes increase blood glucose levels.
  3. Glycogen metabolism releases glucose within liver cells and increases storage of glucose in the form of glycogen. These processes decrease blood glucose levels.
  4. None of the above

Chemistry

Carbon monoxide binds tightly to the heme groups of hemoglobin and myoglobin. How does this affinity reflect the toxicity of carbon monoxide?

  1. Since carbon monoxide binds the heme groups of hemoglobin, it is easily removed or replaced by oxygen. As a result, the effects of oxygen enhancement result in what divers call the “bends.”
  2. Because carbon monoxide binds the heme groups of hemoglobin, it is easily removed or replaced by oxygen. As a result, the effects of oxygen deprivation result in suffocation.
  3. Because carbon monoxide binds tightly to the heme groups of hemoglobin, it is not easily removed or replaced by oxygen. As a result, the effects of oxygen deprivation result in suffocation.
  4. None of the above

Pathophysiology

Which of the following may be a reason to order an ABG on a patient?

  1. The patient suddenly develops shortness of breath
  2. An asthmatic is starting to show signs of tiring
  3. A diabetic has developed Kussmaul’s respirations
  4. All of the above

Pharmacology

How do sulfa drugs selectively kill bacteria while causing no harm to humans?

  1. Folic acid is a vitamin required for the synthesis of a coenzyme needed to make the amino acid methionine and the purine and pyrimidine nitrogenious bases for DNA and RNA and folic acid is produced by humans.
  2. Sulfa drug binds to the enzyme, no product is formed, folic acid is made and the biosynthesis of methionine and nitrogenous bases increases.
  3. Humans are not harmed because they do not synthesize their own folic acid. It is obtained in the diet.
  4. None of the above

Pharmacology

What occurs when glycogen metabolism is stimulated by insulin?

  1. Insulin stimulates glycogen synthase, the first enzyme in glycogen synthesis.
  2. Insulin stimulates glycogen synthase, the first enzyme in glycogen synthesis. It also stimulates removal of glucose from the bloodstream into cells and phosphorylation of glucose by the enzyme glucokinase.
  3. Insulin stimulates glycogen synthase, the first enzyme in glycogen synthesis. It also stimulates uptake of glucose from the bloodstream into cells and phosphorylation of glucose by the enzyme glucokinase.
  4. All of the above

Pharmacology

What is the medical application of cortisone? Cortisone is used to treat:

  1. Rheumatoid arthritis, asthma, gastrointestinal disorders, and a variety of skin conditions.
  2. Kidney disease, high blood pressure, and osteoporosis.
  3. Muscle disorders, tuberculosis, and thyroid disorder.
  4. All of the above

Anatomy

Oxygen saturation is likely to be lowest when an asthmatic with a diagnosis of pneumonia is positioned:

  1. In a high Fowler position
  2. Lying on the left side
  3. Lying on the right side
  4. Lying supine with the head of the bed flat


Chemistry

Laboratory test results indicative of thrombocytopenia, in addition to a low platelet count, would be:

  1. Increased PT
  2. Prolonged bleeding time and poor clot retraction.
  3. Increased aPTT
  4. Decreased RBC count.

Pharmacology

The purposes of epinephrine injection include all of the following except:

  1. Stabilizing mast cell membranes.
  2. Relaxing bronchial smooth muscle.
  3. Supporting arterial blood pressure.
  4. Blocking histamine receptors.

Pharmacology
Therapeutic interventions focused on increasing the oxygen supplied to the heart and decreasing the heart’s demand for oxygen include:

  1. Antiplatelet drugs
  2. Anticoagulants
  3. Morphine sulphate
  4. Thrombolytic drugs

Pharmacology
An intervention that would contribute toward the healing of a peptic ulcer is:

  1. Steroid administration
  2. Blocking or neutralizing of acid secretion
  3. Surgical removal of the ulcer
  4. Intravenous nutritional support

Pharmacology
Aspirin and NSAIDs are causative factors for the development of peptic ulcer disease because they:

  1. Increase acid secretion
  2. Allow proliferation of H. pylori
  3. Damage the mucosal barrier
  4. Alter platelet aggregation

Pharmacology
Your patient is interested in trying medication to improve low mood/depression. All of the following medications might be appropriate except:

  1. Selective serotonin reuptake inhibitors
  2. Amitriptyline
  3. Serotonin and norepinephrine reuptake inhibitors
  4. Benzodiazepines

Anatomy

Ausculation of the chest reveals bilateral fine crackles in the bases bilaterally, indicating:

  1. Right-sided heart failure
  2. Left-sided heart failure
  3. Pneumonia
  4. Acute respiratory distress syndrome

Biology
The signs and symptoms of anemia are all related to what common pathophysiologic feature of the condition?

  1. Increased oxygen consumption by tissues
  2. Decreased blood oxygen content
  3. Vasodilation
  4. A shift in the oxyhemoglobin dissociation curve

Biology
In addition to hypertension, preeclampsia is characterized by:

  1. Nausea and vomiting
  2. Fatigue and lower back pain
  3. Protein in the urine and edema
  4. Retinal changes and rates in the lungs

Biology
Common manifestations of bacterial pneumonia include all of the following except:

  1. Fever
  2. Productive Cough
  3. Tachypnea
  4. Hyperinflation

Biology
Closed drainage systems work to re-expand a lung after pneumothorax by:

  1. Re-establishing the normal negative intrapleural pressure.
  2. Creating a positive pressure in the pleural space
  3. Removing excess fluid from the pleural space so that there is room for lung expansion.
  4. Pulling oxygen into distal air sacs to re-expand lung tissue

Biology
Patients with chronic renal failure usually exhibit:

  1. Bradycardia
  2. Hypokalemia
  3. Hypocalcemia
  4. Hematomas

Biology
The diet of a patient in end-stage kidney disease is restricted in all of the following except:

  1. Fluid
  2. Potassium
  3. Protein
  4. Calories

Anatomy

Which of the following is true of the biological functions of progesterone?

  1. Progesterone is the most important hormone associated with pregnancy.
  2. Progesterone directs male sexual characteristics.
  3. Levels of progesterone increases if the egg is not fertilized.
  4. Levels of progesterone remain stable if the egg is not fertilized.

Anatomy

Which of the following is true of the biological functions of testosterone?

  1. Testosterone is not secreted by the ovaries.
  2. Testosterone is needed for development of female secondary sexual characteristics.
  3. Testosterone stimulates ovulation.
  4. Testosterone is needed for development of male secondary sexual characteristics.

Anatomy

Which of the following is true of the biological functions of estrone?

  1. Estrone is required for proper development of male secondary sexual characteristics.
  2. Level of estrogen degreases if the egg is not fertilized.
  3. Estrone is required for proper development of female secondary sexual characteristics.
  4. Estrone affects only the reproductive organs.

Biology

What is the function of hemoglobin?

  1. Hemoglobin is the protein in red blood cells that is responsible for carrying oxygen to the cells of the body.
  2. Hemoglobin is a lipid in red blood cells that is responsible for carrying oxygen to the cells of the body.
  3. Hemoglobin is a protein in white blood cells that is responsible for carrying oxygen to the cells of the body.
  4. Hemoglobin is a protein in red blood cells that is not responsible for carrying carbon dioxide to the cells of the body.

Biology

Why is heat an effective means of sterilization?

  1. Heat is an effective means of sterilization because it destroys the proteins of microbial lifeforms, including fungi, bacteria, and viruses.
  2. Heat is an effective means of sterilization because it destroys the proteins of anaerobic microbial lifeforms, including fungi, bacteria, and viruses.
  3. Heat is an effective means of sterilization because it destroys the lipids of microbial lifeforms, including fungi, bacteria, and viruses.
  4. Both (B) and (C).

Chemistry:

List the enzymes whose levels are elevated in the blood serum following an MI.

  1. CPK, LDH, AST, and SGOT
  2. LDH, AST, and SGOT
  3. CRE, AST, and ALT
  4. None of the above

Chemistry

What is the physiological function of gluconeogenesis?

  1. Gluconeogenesis is production of glucose from noncarbohydrate molecules in times when blood glucose levels are low. This ensures proper function of brain and red blood cells, which only use glucose as fuel.
  2. Gluconeogenesis is production of glucose from noncarbohydrate molecules in times when blood glucose levels are high. This ensures proper function of brain and white blood cells, which only use glucose as fuel.
  3. Gluconeogenesis is production of glucose from carbohydrate molecules in times when blood glucose levels are low. This ensures proper function of brain and red blood cells, which only use glucose as fuel.
  4. None of the above

Chemistry

What effect does glycogen metabolism have on glucose levels?

  1. Glycogen metabolism traps glucose within liver cells and increases storage of glucose in the form of glycogen. These processes decrease blood glucose levels.
  2. Glycogen metabolism traps glucose within liver cells and increases storage of glucose in the form of glycogen. These processes increase blood glucose levels.
  3. Glycogen metabolism releases glucose within liver cells and increases storage of glucose in the form of glycogen. These processes decrease blood glucose levels.
  4. None of the above

Chemistry

Carbon monoxide binds tightly to the heme groups of hemoglobin and myoglobin. How does this affinity reflect the toxicity of carbon monoxide?

  1. Since carbon monoxide binds the heme groups of hemoglobin, it is easily removed or replaced by oxygen. As a result, the effects of oxygen enhancement result in what divers call the “bends.”
  2. Because carbon monoxide binds the heme groups of hemoglobin, it is easily removed or replaced by oxygen. As a result, the effects of oxygen deprivation result in suffocation.
  3. Because carbon monoxide binds tightly to the heme groups of hemoglobin, it is not easily removed or replaced by oxygen. As a result, the effects of oxygen deprivation result in suffocation.
  4. None of the above

Pathophysiology

Which of the following may be a reason to order an ABG on a patient?

  1. The patient suddenly develops shortness of breath
  2. An asthmatic is starting to show signs of tiring
  3. A diabetic has developed Kussmaul’s respirations
  4. All of the above

Pharmacology

How do sulfa drugs selectively kill bacteria while causing no harm to humans?

  1. Folic acid is a vitamin required for the synthesis of a coenzyme needed to make the amino acid methionine and the purine and pyrimidine nitrogenious bases for DNA and RNA and folic acid is produced by humans.
  2. Sulfa drug binds to the enzyme, no product is formed, folic acid is made and the biosynthesis of methionine and nitrogenous bases increases.
  3. Humans are not harmed because they do not synthesize their own folic acid. It is obtained in the diet.
  4. None of the above

Pharmacology

What occurs when glycogen metabolism is stimulated by insulin?

  1. Insulin stimulates glycogen synthase, the first enzyme in glycogen synthesis.
  2. Insulin stimulates glycogen synthase, the first enzyme in glycogen synthesis. It also stimulates removal of glucose from the bloodstream into cells and phosphorylation of glucose by the enzyme glucokinase.
  3. Insulin stimulates glycogen synthase, the first enzyme in glycogen synthesis. It also stimulates uptake of glucose from the bloodstream into cells and phosphorylation of glucose by the enzyme glucokinase.
  4. All of the above

Pharmacology

What is the medical application of cortisone? Cortisone is used to treat:

  1. Rheumatoid arthritis, asthma, gastrointestinal disorders, and a variety of skin conditions.
  2. Kidney disease, high blood pressure, and osteoporosis.
  3. Muscle disorders, tuberculosis, and thyroid disorder.
  4. All of the above

Anatomy

Oxygen saturation is likely to be lowest when an asthmatic with a diagnosis of pneumonia is positioned:

  1. In a high Fowler position
  2. Lying on the left side
  3. Lying on the right side
  4. Lying supine with the head of the bed flat


Chemistry

Laboratory test results indicative of thrombocytopenia, in addition to a low platelet count, would be:

  1. Increased PT
  2. Prolonged bleeding time and poor clot retraction.
  3. Increased aPTT
  4. Decreased RBC count.

Pharmacology

The purposes of epinephrine injection include all of the following except:

  1. Stabilizing mast cell membranes.
  2. Relaxing bronchial smooth muscle.
  3. Supporting arterial blood pressure.
  4. Blocking histamine receptors.

Pharmacology
Therapeutic interventions focused on increasing the oxygen supplied to the heart and decreasing the heart’s demand for oxygen include:

  1. Antiplatelet drugs
  2. Anticoagulants
  3. Morphine sulphate
  4. Thrombolytic drugs

Pharmacology
An intervention that would contribute toward the healing of a peptic ulcer is:

  1. Steroid administration
  2. Blocking or neutralizing of acid secretion
  3. Surgical removal of the ulcer
  4. Intravenous nutritional support

Pharmacology
Aspirin and NSAIDs are causative factors for the development of peptic ulcer disease because they:

  1. Increase acid secretion
  2. Allow proliferation of H. pylori
  3. Damage the mucosal barrier
  4. Alter platelet aggregation

Pharmacology
Your patient is interested in trying medication to improve low mood/depression. All of the following medications might be appropriate except:

  1. Selective serotonin reuptake inhibitors
  2. Amitriptyline
  3. Serotonin and norepinephrine reuptake inhibitors
  4. Benzodiazepines

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Analysis of a Biotechnology Company

Analysis of a Biotechnology Company - Intellect Neurosciences, Inc.
Analysis of a Biotechnology Company – Intellect Neurosciences, Inc.

Analysis of a Biotechnology Company – Intellect Neurosciences, Inc.

Biological knowledge required
Company name: Intellect Neurosciences, Inc.
Website: http://www.intellectns.com
The suggested content, assessment criteria, format, and referencing style will be uploaded in another word file.

Your work must be:-

  • Word processed / typed
  • Size 12 font e.g. Times New Roman or Arial
  • Double line spaced
  • Right hand margin 20 mm / 0.75”
  • Left hand margin 40mm / 1.5”
  • Double sided
    Page numbered from the title page in the format ‘Page 1 of 1’
  • Reference list – single line spacing
  • Appendices – single line spacing if possible

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New law on biomedical scientists and biomedical research

New law on biomedical scientists and biomedical research
New law on biomedical scientists and biomedical research

Use your knowledge of the current ethical, professional and commercial paradigms of biomedical research to discuss the ramifications of the new law on biomedical scientists and biomedical research.

It’s the year 2024 And the world has changed over the last 10 years. In response to pressure from lobby
groups, the Australian Parliament is poised bring into effect new law:
The use of any animals in medical research will be banned. The move has been lauded by animal welfare groups, but many suspect that the push for the law has come from ‘anti-science’ elements within the government.Write essay. In essay, assume the law above has come into effect. Use your knowledge of the current ethical, professional and commercial
paradigms of biomedical research to discuss the ramifications of the new law on biomedical scientists and biomedical research.

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