Bisc 344 - Clinical Chemistry And Toxicology

Front 1

What is the primary goal of instrumental analysis?

Back 1

To perform tests with the highest degree of accuracy and precision as possible

Front 2

List the steps in all clinical testing.

Back 2

1. Select Test

2. Collect and preserve specimen

3. Select Method

4. Adhere to QC

5. Perform Test/Evaluate and Report Results

6. Correlate results

Front 3

List the federal requirements for analytical methods evaluation

Back 3

1. Write protocols for instrument evaluation

2. Document the validity of the procedure

3. Report the range of accuracy by analyzing a series of samples of known values

4. Determine the precision of the instrument and method

5. Estimate the sensitivity of the instrument and method

6. Test the instrument and method

7. Establish reference intervals

8. Validate above results

9. Prepare inservice training materials

IN SUMMARY, validate:

1. Procedure materials

2. QC Methods

3. Maintenence methods

4. Personnel

Front 4

Name the two kinds of error.

Back 4

Random and Systematic

Front 5

This type of error can be present in all measurements, can be positive or negative, and can be due to an instrument, operator, reagent, or environment variation

Back 5

Random Error

Front 6

This type of error influences observations consistently in one direction. It should not be present in a method. The measure of location, the slope, y intercept can all provide measures of this type of error.

Back 6

Systematic

Front 7

Name the two types of systematic error

Back 7

Constant and proportional

Front 8

This type of error exists where there is a difference between the test method and the comparative method, regardless of concentration, as reflected by the y intercept.

Back 8

Constant error

Front 9

This type of error exists when the differences between the test method and comparative method are relative to the concentration, indicated by a slope that is different than 1.

Back 9

Proportional error

Front 10

How many reference values should be included in a reference range study?

Back 10

At least 120

Front 11

This term is used to describe an error made because of "bad" reagents.

Back 11

Analytic error

Front 12

This is a federal law that requires all laboratories to perform specific evaluations of methods before patient laboratory test results can be reported.

Back 12

CLIA

Front 13

The following components are found in this.

1. Procedure name

2. Clinical Significance

3. Principle of Method

4. Specimen requirements

5. Reagent and equipment

6. Step by step procedure

7. Reference range

8. Comments

9. References

Back 13

SOP (Student Operating Procedures)

Front 14

This is a measurement that describes the reproducability of results

Back 14

Precision

Front 15

What bonds do all carbohydrates form?

Back 15

C=O and -OH

Front 16

Most sugars are this configuration.

Back 16

D

Front 17

List three monosaccharides.

Back 17

Glucose, Fructose, Galactose

Front 18

List three disaccharides.

Back 18

Maltose, Lactose, Sucrose.

Front 19

This is a word meaning the chaining of two to ten sugar units.

Back 19

Oligosaccharides

Front 20

This is a word meaning more than ten sugar units in a chain.

Back 20

Polysaccharides

Front 21

This is a substance made of glucose molecules.

Back 21

Starch

Front 22

This is the storage form of glucose.

Back 22

Glycogen

Front 23

Describe the steps in the glycolysis pathways.

Back 23

1. Convert glucose to G6P using ATP (catalyzed by hexokinase)

2. G6P can enter the Embden-Myerhof pathway or the hexose monophosphate pathway (energy production) OR it can be converted to glycogen (storage)

3a. Embden-Meyerhof pathway - Glucose is broken down into two 3 carbon molecules of pyruvic acid which enters the TCA and is converted into acetyl coA. Fatty acids, ketones, and some animo acids are converted to acetyl coA also. (AEROBIC) (Gluconeogenesis - conversion of amino acids, glycerol lactate, or pyruvate to glucose)

3b. 6GP is converted into 6PA and ends in NADPH production. Glucose can be stored as glycogen or converted back into G6P

Front 24

This is the conversion of amino acids, glycerol lactate, or pyruvate to glucose.

Back 24

Gluconeogenesis

Front 25

When the body's energy requirements are met, glucose can be stored as glycogen in this process.

Back 25

Glycogenesis

Front 26

This is a process in which glycogen is converted back to glucose-6-phosphate.

Back 26

Glycogenolysis

Front 27

When alternate sources of energy production are used (glycerol, lactic acid, amino acids), these form in the blood.

Back 27

Ketone Bodies

Front 28

Organs with endocrine involvement in glucose metabolism are:

Back 28

Liver, pancreas, others (thyroid)

Front 29

Two major hormones for glucose control from pancreas with opposite actions

Back 29

Insulin and Glucagon

Front 30

This is the primary hormone responsible for entry of glucose into cells of the body. It causes movement of glucose from blood into cells, decreasing levels in the blood.

Back 30

Insulin

Front 31

This is the primary hormone for increasing glucose levels. It is a hyperglycemic agent, meaning that it increases blood glucose by stimulating glycogen breakdown and production of glucose from non-carb sources. It is released during stress or fasting states

Back 31

Glucagon

Front 32

This hormone comes from the adrenal gland and increases plasma glucose by inhibiting insulin secretions in the pancreas.

Back 32

Epinephrine

Front 33

This hormone comes from the adrenal gland. Produced in response to ACTH and increases plasma glucose.

Back 33

Cortisol

Front 34

This hormone increases glucose by decreasing its entry into the cells. Comes from anterior pituitary

Back 34

Growth hormone

Front 35

This is released from the anterior pituitary gland in response to low cortisol levels

Back 35

ACTH

Front 36

This hormone increases glucose levels and comes from the thyroid gland.

Back 36

Thryoxine

Front 37

This hormone increases glucose, inhibits insulin, and is formed in the delta cells of the islets of lagerhans.

Back 37

Somatostatin

Front 38

This is the metabolism of glucose to pyruvate or lactate for the production of energy.

Back 38

Glycolysis

Front 39

This is the formation of G5P for noncarb sources.

Back 39

Gluconeogenesis

Front 40

This is the breakdown of glycogen to glucose for use as energy

Back 40

Glycogenolysis

Front 41

This is the conversion of glucose to glycogen for storage

Back 41

Glycogenesis

Front 42

This is the conversion of carbs to fatty acids

Back 42

Lipogenesis

Front 43

This is the decomposition of fats.

Back 43

Lipolysis

Front 44

This is an increase in plasma glucose levels and is sustained by imbalanced hormones.

Back 44

Hyperglycemia

Front 45

This type of diabetes is associated with problems with secretion of insulin in beta cells. The lack of insulin results in hyperglycemia and only 10% of diabetics are this type. Onset is acute and they are dependent on insulin. Tend to develop ketosis.

Back 45

Type 1

Front 46

Describe laboratory results for Type I Diabetes

Back 46

-Glucose increased (70-110 mg/dl)

-Glucosuria when plasma is above 180 mg/dl

-Ketones often produced (absence of insulin, excess glucagon)

-Ketoacidosis bc of dehydration

Front 47

This type of diabetes is associated with resistance to insulin with insulin secretory defect. Most diabetics are this type, are obese, and have increased abdominal fat. It can go undiagnosed for years, symptoms are mild, and onset occurs during adulthood. Individuals suffer from circulatory and nervous complications.

Back 47

Type 2 Diabetes

Front 48

Describe the lab results for Type 2 Diabetes.

Back 48

-Increased glucose

-Glucosuria

-Ketones are NOT present

-Complication = kidney damage

Front 49

This type of diabetes occurs during pregnancy. Changes include metabolic and hormonal changes and many patients return to normal afterwards, but remain at a high risk later.

Back 49

Gestational Diabetes

Front 50

What are the infant risks during gestational diabetes?

Back 50

-Respiratory disease

-Hypocalcemia

-Hyperbilirubinemia

Front 51

This is when plasma glucose levels are below 50 mg/dl. Glucagon is released from the pancreas and insulin is inhibited. Epinephrine is released and glucose metabolism is is increased. Insulin is inhibited

Back 51

Hypoglycemia

Front 52

Describe the lab results for hypoglycemia.

Back 52

-Glucose levels decreased

-Insulin levels will be extremely elevated

Front 53

This disease refers to a defect in the metabolic pathways that convert glycogen back to glucose. There's an enzyme deficiency of G6P resulting in lots of ketones, lactase and alanine. Glycogen builds up in the liver causing hepatomegaly

Back 53

Von Gierke's Disease

Front 54

This glucose oxidase method is validated by a color change

Back 54

Trinder method

Front 55

This is the most accurate glucose testing method.

Back 55

Hexokinase

Front 56

What are the two major roles of lipids/fats?

Back 56

Rich source of energy and are an integral part of cell membranes

Front 57

Describe the lipid structure.

Back 57

Chain of C-H bonds that end with a -COOH

Front 58

How are fatty acids classified?

Back 58

-Saturated - bonded with H ions

-Mono-unsaturated - one double bond

-Poly-unsaturated - two or more double bonds

Front 59

What are the differences between cis and trans fatty acids?

Back 59

-Cis have the H atoms on the same side, causing a bend in the structure. They are fluids.

-Trans have no bend in the structure and they are usually solids

Front 60

Describe the differences in saturated and unsaturated fatty acids with regards to packaging.

Back 60

Saturated fatty acids can be packed together tightly (solids) - animal sources

Unsaturated fatty acids have kinks in their structures (oils) - plant sources

Front 61

How are phospholipids and triglycerides different?

Back 61

Phospholipids have two fatty acids and one phospholipid group.

Front 62

This is an unsaturated steroid alcohol containing four rings with a single C-H side chain tail

Back 62

Cholesterol

Front 63

These are like tanker trucks, carrying triglycerides assembled in the liver out to the cells for energy needs or storage as fats.

Back 63

VLDLs

Front 64

These are rich in cholesterol and represent almost empty tankers that deliver cholesterol after triglycerides have been loaded off.

Back 64

LDLs

Front 65

This is the cleanup grew, gathering up extra cholesterol for transport back to the liver.

Back 65

HDL

Front 66

These are the tankers that deliver fuel throughout the body, finally docking in the liver to deposit remnants.

Back 66

Chylomicrons

Front 67

These are the largest lipoproteins in diameter and create turbidity when present in serum. They are very light and will float to the top of stored plasma creating a creamy layer.

Their primary role is to deliver dietary lipids to the liver and peripherial cells

Back 67

Chylomicrons

Front 68

These lipoproteins are produced by the liver and are very rich in triglycerides. They are the major carrier of liver-derived triglycerides and transport triglycerides from the liver to the tissues.

They can create turbidity in the serum but do not float to the top. They are increased due to dietary intake of carbs, saturated fatty acids and trans fatty acids.

Back 68

VLDL

Front 69

These are the most cholesterol rich lipoproteins, formed by the lipolysis of VLDL. They are smaller than VLDL and chylomicrons and can infiltrate extracellular spaces, allowing them to be ingested by microphages.

Back 69

LDL

Front 70

Macrophages with too much lipid are called this.

Back 70

Foam cells

Front 71

These are the smallest and most dense lipoproteins. They can remove cholesterol from cells and deliver it to the liver.

Back 71

HDL

Front 72

This is a lipid disease that is the single leading cause of death and disability, resulting from lipid deposits in the artery walls.

Back 72

Arteriosclerosis

Front 73

This lipid disease is inherited and predisposes one to elevated cholesterol levels, mostly LDL, because these people lack LDL receptors. NOTE: LDL buildup can cause coronary heart disease.

Back 73

Hypercholesterolemia

Front 74

This lipid disease results from an imbalance between synthesis and clearance of VLDL in circulation.

Back 74

Hypertriglyceridemia

Front 75

Amino acids are composed of:

Back 75

-Amino group (-NH2)

-Carboxyl Group (-COOH)

-Differing side chains

Front 76

How many amino acids are used for protein building?

Back 76

20

Front 77

Where are the amino acids absorbed?

Back 77

Into the blood stream through the intestines

Front 78

This is a disorder that occurs in 1/15,000 births, caused by the absense of phenylalanine hydroxylase

Back 78

PKU (Phenylketonuria)

Front 79

What bonds join amino acids to form proteins?

Back 79

Peptide bonds

Front 80

How many amino acids are in the average polypeptide chain?

Back 80

100-150

Front 81

This protein structure is the base structure, crucial for function and molecular characteristics. Any change will result in an altered, dysfunctional protein.

Back 81

Primary structure

Front 82

This protein structure refers to the winding of the polypeptide chain itself, forming hydrogen bonds between NH and CO groups. Can be alpha helix or beta sheet.

Back 82

Secondary structures

Front 83

This protein structure refers to the twisting and folding of chains caused by R-group interactions. Bonds are disulfide, electrostatic, hydrogen, hydrophobic, or van der Waals.

Back 83

Tertiary structure

Front 84

This protein structure refers to the arrangement of two or more polypeptide chains to form the functional protein. Example: hemoglobin

Back 84

Quaternary structure

Front 85

This refers to the secondary, tertiary, or quatenary structure disturbance of the protein, resulting in lost functionality, caused by heat, hydrolysis, enzymes, or exposure to urea or UV light.

Back 85

Denaturation

Front 86

Proteins are comprised of what elements? What element sets proteins apart from carbs or lipids?

Back 86

Carbon, nitrogen, oxygen, hydrogen, sulfur; nitrogen

Front 87

Where are most proteins synthesized? What is the exception?

Back 87

Liver; the exception is immunoglobulins synthesized in plasma cells.

Front 88

How are proteins synthesized?

Back 88

-DNA is unzipped

-One strand is used as a template to form complementary mRNA

-mRNA carries genetic code from DNA, moves to cytoplasm, and attaches to ribosomes

-A codon (3 bases) is attached to the mRNA to specify which amino acid is to be transcribed

-tRNA seeks out the amino acid needed and delivers it to the ribosome

-Each tRNA delivers the acid needed, attaching it via peptide bond to the previous amino acid

-When the terminal codon is reached, the peptide chain detaches and the ribosome and mRNA dissociate

Front 89

What are some of the functions of proteins?

Back 89

Nutrition source

Water distribution

pH balancing buffer

Transportation

Antibodies

Receptors for hormones

Enzymes

Connective tissue structure

Coag and hemostasis of blood

Front 90

This plasma protein migrates ahead of albumin on electrophoresis and carries thyroid hormones. Low levels indicate poor protein nutritional status.

Back 90

Prealbumin

Front 91

This protein is present in the highest concentration in serum. It is synthesized in the liver and has two major functions: transport protein and maintenance of osmotic pressure.

Decreased levels: malnutrition, liver disease, loss in urine bc kidney disease

Increased levels: dehydration

Back 91

Albumin

Front 92

These plasma proteins consist of alpha1, alpha2, beta and gamma fractions.

Back 92

Globulins

Front 93

This plasma protein neutralize trypsin-like enzymes that damage proteins.

Back 93

Alpha 1 antitrypsin

Front 94

This plasma protein is synthesized in the fetal yolk sack and is not found in adults. Fetal distress causes its increase. Decreased levels can indicate down's syndrome

Back 94

Alpha fetoprotein

Front 95

This plasma protein is also known as Alpha2 glycoprotein, made in the liver; binds to free hemoglobin. Increased in inflammation.

Back 95

Haptoglobin

Front 96

This plasma protein contains copper and is an alpha2 glycoprotein. It functions as an enzyme and 90% of serum copper is found in this. Low levels result in copper deposited in skin, liver, brain, and cornea (Kayser-Fleischer rings) in Wilson's Disease.

Back 96

Ceruloplasmin

Front 97

This plasma protein is very large and made in the liver. It cannot move well due to its large size and it inhibits proteases. Increased by the use of contraceptives, pregnancy, diabetes, liver disease

Back 97

Alpha2 macroglobulin

Front 98

This plasma protein is a glycoprotein synthesized in the liver. Can bind to two ferric iron molecules. Main function is iron transport and iron loss prevention. It transports ion to storage sites (converted to ferritin) and to bone marrow (hemoglobin synthesis)

Back 98

Transferrin

Front 99

This plasma protein is the light chain of HLA found on the surface of lymphocytes. It's small and filtered by the glomerulus. Increased levels suggest kidney disease, inflammatory disease, or diseases with large lymphocyte turnover.

Back 99

Beta2 microglobulin

Front 100

This term is used for several proteins that participate in immune reactions and serve as a link to the inflammatory response. They circulate in the blood as precursors until they are activated.

Back 100

Complement

Front 101

One of the largest proteins, made in the liver. It is seen between beta and gamma regions. They form a clot when activated by thrombin.

Back 101

Fibrinogen

Front 102

What are the five major groups of immunoglobulins?

Back 102

IgA, IgG, IgM, IgD, IgE

Front 103

Which immunoglobulin is synthesized in the neonate only?

Back 103

IgM

Front 104

Describe the immunoglobulin structure.

Back 104

-Two long polypeptide chains (heavy)

-Two short polypeptide chains (light)

-Joined by disulfide bonds

Front 105

The heavy chains of each immunoglobulin are:

Back 105

IgG - gamma

IgA - alpha

IgM - Mu

IgD - Delta

IgE - Elipson

(named for their heavy chains, obviously)

Front 106

What causes an increase in IgG? Decrease?

Back 106

Increase:

-Liver Disease

-Infections

-Collagen Diseases

Decreases:

-Susceptibility to infection

Front 107

This immunoglobulin is present in respiratory and GI mucosa. Can be found in secretions.

Back 107

IgA

Front 108

What causes an increase in IgA?

Back 108

Liver disease, infections, autoimmune disease

Front 109

This is the first immunoglobulin/antibody to appear in response to antigenic stimulation.

Back 109

IgM

Front 110

What causes an increase in IgM?

Back 110

Toxoplasmosis, cytomegalovirus, herpes, rubella, syphilis, various bacterial diseases, fungal diseases

*Monoclongal IgM increase: Waldenstrom's Macroglobulinemia

Front 111

What causes an increase in IgD?

Back 111

Infection, liver disease, connective tissue disorders

Front 112

What causes an increase in IgE?

Back 112

Allergic and anaphylactic reactions

Front 113

This protein is a heme protein found in striated skeletal and cardiac muscle. Most is dissolved into cytoplasm of cells. 1/4 size of hemoglobin and can bind to oxygen.

Back 113

Myoglobin

Front 114

This is a complex of three proteins that bind to the thin filaments of striated muscle that work together to regulate muscle contraction.

Back 114

Troponin

Front 115

This is the classical method of measuring total nitrogen. It is precise and accurate, used as a reference method, but not routinely used in clinical labs.

Back 115

Kjedahl