Amino Acids and Proteins Flashcards

1
Q

Define the following terms: Isoelectric point

A

pH at which a molecule carried no net charge.

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2
Q

Define the following terms: Zwitterion

A

moments of differing charge but net neutral

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3
Q

Define the following terms: Amphoteric

A

serves as both an acid and base

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4
Q

Define the following terms: Amino acid

A

essential molecules that build protein

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5
Q

Define the following terms: Peptide bond

A

from acid group to amino groupof two animo acids

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6
Q

Define the following terms: Complex or conjugated protein

A

more than 1 combined tertiary structure

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7
Q

Discuss protein structures and classifications

A

Size: 6k-1m Da
Differential Solubility
Charge (more pos more easily disolved)
Adsorption (ability for water to cling to)
Specific binding to antibodies
Made of C, O, H, N, S. N sets apart from lipids and carbohydrates.

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8
Q

Differentiate among protein structures:

Primary

A

Chain of amino acids

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9
Q

Differentiate among protein structures:

Secondary

A

Linked by H-bonds. Beta sheets and Alpha helices. Alpha more common.

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10
Q

Differentiate among protein structures:

Tertiary

A

Formed when attractions occur between the sheets and helices. Function is related to folding structure

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11
Q

Differentiate among protein structures:

Quaternary

A

multiple tertiary structures together. Think Hemoglobin.

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12
Q

Explain the process of digestion and absorption of dietary proteins

A

Pepsin breaking proteins into peptides. Peptides are broken into Amino acids by secretin in the intestines. Pancreas Acinar cells secrete enzymes to assist

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13
Q

State the main physiologic functions of plasma proteins

A

Albumin: 54%
Globulins: 46%
Total protein - albumin = Globulins

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14
Q

Identify the main site of synthesis for plasma proteins

A

Prealbumin: Liver and choroid plexus
Albumin: liver

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15
Q

Discuss the degradation of amino acids

Transamination and oxidative deamination

A

Transamination: the transfer of an amino group from one molecule to another
deamination: the removal of an amino group from an amino acid or other compound

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16
Q

Discuss the degradation of amino acids

Ketogenic and glycogenic amino acids

A

Ketogenic: can be oxidized to generate acetyl-CoA

glycogenic amino acids: an amino acid that can be converted into glucose

17
Q

State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels

Albumin

A

Function: oncotic pressure
Disease: Liver disease, renal disease, dehydration, malnutrition

18
Q

State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels

Alpha-1-antitrypsin

A

Synthesized in: liver
protects elastin in the lungs by inhibiting elastase
diseases: inflammitory disease

19
Q

State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels

Alpha-2-macroglobulin

A

synthesized in the liver
serine protease inhibitor
Decreased in: acute pancreatitis, prostate cancers, inflam disorders
Increased in: nephrotic syndrome, contraceptive use, pregnancy and estrogen therapy

20
Q

State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels

Haptoglobin

A

Function: transport protein (free hemoglobin)
increased in: inflam disease, burns, trauma
Decreased in: intravascular hemolysis, liver disorders

21
Q

State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels

Ceruloplasmin

A

function: transport protein (copper)
increaded in: inflam, severe infection, tissue damage
Decreased in: (primary) Wilson’s disease. (secondary) malnutrition/malabsorption, liver disease, nephrotic syndrome

22
Q

State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels

Transferrin

A

Function: transport protein (iron)
increased: Iron deficiency
decreased: iron overload

23
Q

State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels

Fibrinogen

A

Function: clot when activated by thrombin
increased: infection, pregnancy
decreased: coagulation

24
Q

State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels

C-reactive protein

A

Function: stimulates tissue factor, causing coagulation and activating complement
Should be none
increased: tissue damage

25
Q

Correlate disease states and disorders associated with total protein levels and other test results

A

Hypoproteinemia: TP less than ref range. Any condition with a negative Nitrogen balance. Caused by excessive loss, decreased intake/synthesis, or accelerated breakdown of proteins

Hyperproteinemia: TP greater than ref range. Caused by dehydration or overproduction of gamma globulins

26
Q

State the reference range for serum total protein and albumin.

A

TP: 6.5-8.3 g/dl in adults
Albumin 3.5-5.5 g/dl