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Clinical Chemistry-MIDTERMS > Proteins > Flashcards

Proteins Flashcards

1
Q

-simple organic compounds that serve as the building blocks of proteins

A

AMINO ACIDS

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2
Q

-Amino acids are amphoteric and classified as__________

A

ZWITTERIONS

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3
Q

-formed when the carboxyl group on one amino acid links to the amino group of another amino acid with the loss of a water molecule

A

PEPTIDE BOND

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4
Q

-End of protein structure with a free amino group

A

N-TERMINAL

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5
Q

-End of protein structure with a free carboxyl group

A

C-TERMINAL

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6
Q

-at low pH

A

CATION

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7
Q

-at high pH

A

ANION

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8
Q
  1. It helps to grow and repair body tissues
  2. Maintain the myelin sheaths that protect nerve cells
  3. Serves as the precursor for several hormones end
A

HISTIDINE

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9
Q

Branched chain amino acid group

A

ISOLEUCINE, LEUCINE, AND VALINE

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10
Q

-concentrated in muscle tissues and essential for wound healing, immune function, glucose hemostasis, and hemoglobin formation

A

ISOLEUCINE

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11
Q

-regulation of blood glucose, wound healing, and prevention of muscle protein degradation

A

LEUCINE

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12
Q

-promotes mental health and muscle coordination

A

VALINE

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13
Q
  1. Production of antibodies and maintaining healthy tissues
    2.Helps in the absorption and conservation of calcium
  2. Serves an important role in the formation of collagen
A

LYSINE

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14
Q
  1. helps to initiate the translation of messenger RNA, stabilizes protein structure, and important cellular antioxidant
  2. it is an important source of sulfur for normal metabolism and growth
  3. Assists in the breakdown of fats, and detoxifies lead and other heavy metals
  4. Helps to diminish muscle weakness and prevents brittle hair
A

METHIONINE

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15
Q
  1. metabolic precursor for tyrosine-essential for the production of dopamine horepinephrine, and epinephrine.
A

PHENYLALANINE

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16
Q
  1. Important component in the formation of collagen, elastin, and tooth enamel
  2. important production of neurotransmitters and overall health of the nervous system.
  3. Helps to maintain proper protein balance, aids liver function and metabolism of porphyrins
A

THREONINE

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17
Q
  1. Metabolic precursor for serotonin and melatonin which regulate appetite, mood, sleep, and pain
  2. Natural relaxant that helps alleviate insomnia, and soothes anxiety, and depression
  3. Essential for the production of niacin
A

TRYPTOPHAN

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18
Q
  1. Major role in the transfer of nitrogen from peripheral tissues to the liver for processing and excretion and strengthens the immune system by antibodies
  2. Serves as a source of energy for the central nervous system
  3. Helps in reducing the buildup of toxic substances released when muscle protein is broken down
A

ALANINE

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19
Q
  1. Plays an important role in the synthesis of ammonia
  2. The primary function is the conversion of one amino acid into another via amination or transamination
A

ASPARAGINE

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20
Q
  1. Serve as the precursor for several other amino acids, such as asparagine, arginine, lysine, methionine, threonine, and isoleucine
A

ASPARTIC ACID OR ASPARTATE

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21
Q
  1. Produced from the transamination of amino acids such as alanine and aspartic acid
  2. Serves as neurotransmitter and has important role in the metabolism of CHO and fats
A

GLUTAMIC ACID OR GLUTAMATE

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22
Q
  1. Unlike other amino acids, it is not directly coded in the genetic code, rather it is encoded to UGA codon.
  2. Only one synthesized on its tRNA in all domains of life
  3. Only amino acid containing an essential dietary micronutrient (selenium) as a constitutive component
A

SELENOCYSTEINE

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23
Q
  1. Need for the proper metabolism of lipids and fatty acids
  2. Plays an important role in the synthetic pathways of pyrimidines, purines, creatinine, and porphyrins serve as a component of the protective myeline sheaths surrounding nerve fibers
  3. Aids in the production of antibodies
A

SERINE

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24
Q
  1. Plays an important role in cell division, wound healing, stimulation of protein synthesis, immune function, and the release of hormone.
  2. Conversion of ammonia to urea
A

ARGININE

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25
Q
  1. Synthesized from glutamic acid with an addition of ammonium group and donate the ammonium group form urea
  2. Renal maintenance of the acid-base balance, providing fuel for healthy digestive tract and basis of the building blocks for synthesis of RNA and DNA
A

GLUTAMINE

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26
Q
  1. Potentially toxic so it is absorbed during digestion to convert into cystine-more stable in the G.I tract and less toxic
  2. Important structural and functional component for proteins
    Found in beta-keratin and is important in collagen formation
A

CYSTEINE

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27
Q
  1. Essential for synthesis of nucleic acids, proteins, peptides, purines, ATP, porphyrins, hemoglobin, glutathione, creatine, bile salts, glucose, glycogen, and other amino acids
  2. Limits muscle degeneration, improves glycogen storage, promotes healing, detoxification in the liver.
A

GLYCINE

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28
Q
  1. Produced from glutamic acid and other amino acids
  2. Serves as precursor for hydroxyproline-manufactured in collagen, ligaments, and cardiac tissues, tendons.
  3. Involves wound healing especially the cartilage, strengthening of joints, tendons, and cardiac tissues.
A

PROLINE

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29
Q
  1. Serves as a precursor for adrenal and thyroid hormones.
  2. Stimulates metabolism and the nervous system, acts as a mood elevator and aids in function of the adrenal, thyroid, and pituitary glands.
A

TYROSINE

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30
Q

Proteins comes from the greek word_________ meaningf “first rank of importance”

A

proteios

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31
Q

Large molecules referred to as:

A

MACROMOLECULES

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32
Q

Fundamental building block or protein:

A

AMINO ACIDS

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33
Q

Protein soluble in water is:

A

ALBUMIN

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34
Q

Element that distinguishes protein from CHO and Lipids is:

A

NITROGEN

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35
Q

participation as buffers to maintain pH

A

Acid-base balance

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36
Q

part of immune defense system

A

Antibodies

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37
Q

hormones and receptors

A

Hormones

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38
Q

connective tissue

A

Structure

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39
Q

catalyst

A

Enzymes

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40
Q

participation in coagulation of blood

A

Hemostasis

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41
Q
  1. it is the linear sequence of the amino acids
  2. Any change in the amino acid composition can significantly alter the protein
A

PRIMARY STRUCTURE

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42
Q

It involves the winding of the polypeptide chain

A

SECONDARY REACTION

43
Q
  1. It is the actual three-dimentional configuration; the folding pattern of proteins
  2. It is responsible for many of the physical and chemical properties of proteins
A

TERTIARY STRUCTURE

44
Q

It is the association of two or more polypeptide chains to form a functional protein molecule

A

QUATERNARY STRUCTURE

45
Q

It is a balance between anabolism (synthesis) and catabolism (breakdown)

A

NITROGEN BALANCE

46
Q
  1. This happens when more nitrogen is incorporated in the body than excreted
    ex: pregnant women, growing children, and adults recovering from major illness
A

POSITIVE NITROGEN BALANCE

47
Q
  1. Happens when more nitrogen is excreted than is incorporated into the body
    ex: burns, wasting diseases, continual high fever, and starvation
A

NEGATIVE NITROGEN BALANCE

48
Q

degrades extracellular proteins

A

LYSOSOMAL PATHWAY

49
Q

degrades important intracellular proteins

A

CYTOSOLIC PATHWAY

50
Q

central reaction that remove amino acid nitrogen from the body or removal of nitrogen from free amino acids

A

TRANSAMINATION

51
Q
  1. Removal of amine group from a molecule. Enzyme which catalyze this reaction are deaminases
  2. In the human body, deaminaton takes place primarily in the liver, however glutamate is also deaminated in the kidneys
A

DEAMINATION

52
Q

Form of amino acid with two differing charges and with a net charge of zero

A

ZWITTERION

53
Q

The pH value at which the sum of a molecule’s charges equals zero

A

ISOELECTRIC POINT

54
Q
  1. A term used to describe the loss of the native or naturally occuring folded structure of proteins.
A

DENATURATION

55
Q

Types of Denaturation

A
  1. HEAT
  2. CHEMICAL
  3. MECHANICAL
56
Q

Contain peptide chains composed of amino acids linked by peptide bonds

A

SIMPLE PROTEINS

57
Q
  1. It migrates ahead of albumin
  2. migrates most anodally (toward the positive pole)
  3. It is used as a landmark to confirm that the specimen is CSF; it crosses more easily into the CSF rather than other proteins
A

PREALBUMIN/TRANSTHYRETIN

58
Q

Method for measurement of prealbumin

A

Nephelometry

59
Q

Reference range of prealbumin

A

18-45 mg/dl

60
Q
  1. It is the most abundant protein in plasma
  2. It is a general transport protein and buffers pH and is negative acute-phase reactant protein
  3. It maintains osmotic pressure
  4. It is an indicator of nutritional status
  5. Affects the half-life of drugs
61
Q

Method for measurement of Albumin

A

Dye Methods

62
Q

What is the two dye methods

A

bromcresol green and bromcresol purple

63
Q

reference range of albumin

A

3.5-5.0 g/dl

64
Q

severe manifestation of protein-energy malnutrition (PEM)

65
Q

-It is a group of proteins consisting of a1, a2, B, and y fractions
- It is usually measured by subtracting the value of serum albumin from the total protein concentration.

66
Q

Method for measurement of Globulin

A

Indirect method

67
Q

Reference range for globulin

A

2.3-3.5 g/dl

68
Q
  1. Acute ohase reactant
  2. Protease inhibitor
  3. 90% of a a1-globulin band
  4. Inactivates trypsin and other proteolytic enzymes
  5. The most abundant acute phase reactant
A

Alpha-1 antitrypsin

69
Q

Reference Value for Alpha-1 antitrypsin

A

145-270 mg/dl

70
Q
  1. It is a glycoprotein that migrates between albumin and a-1 globulin band
  2. It is the most abundant protein in fetal serum
  3. It peaks in the fetus at 13 weeks of gestation
  4. Serve as tumor marker
A

Alpha-1 fetoprotein

71
Q

Reference Value for Alpha-1 fetoprotein

72
Q
  1. AKA: Orosomucoid
  2. A major plasma glycoprotein that is negatively charged
  3. Produced by the liver
  4. An acute phase reactant
  5. Useful diagnostic tool in neonatal bacterial infection (NOT WIDELY USED)
A

Alpha-1 acid glycoprotein

73
Q

Transports Lipids (HDL)

A

Alpha-1 Lipoprotein

74
Q
  1. Serine protease inhibitor
  2. Binds and inactivates pancreatic elastase, mast cell, chymase, and chymotrypsin
  3. Associated with the pathogenesis of Alzheimer’s disease because it is an integral component of the amyloid deposits
A

Alpha-1 Antichymotrypsin

75
Q

Reference Range for Alpha-1 Antichymotrypsin

A

30-60 mg/dl

76
Q

Inhibits serine proteases

A

Inter-a-trypsin inhibitor

77
Q
  1. Produced by hepatocytes
    2.Major carrier protein of Vitamin D
  2. Transports Vitamin D and bind actin
  3. Important in bone formation and immune system
A

Gc-Globulin/Group Specific component (Gc)

78
Q
  1. Synthesize by the hepatocytes
  2. Evaluate hemolytic anemia
  3. Binds free hemoglobin to prevent urinary loss
  4. Useful marker for hemolysis and hemoglobinuria
  5. Independent risk factor for CVD
  6. Used for paternity testing
A

HAPTOGLOBIN

79
Q

Reference Range for Haptoglobin

A

26-185 mg/dl

80
Q
  1. Copper-carrying protein with enzymatic activities
  2. 90% of copper bound to ceruloplasmin
  3. Marker for Wilson’s disease
A

CERULOPLASMIN

81
Q

Reference Value for Ceruloplasmin

A

18-45 mg/dl

82
Q
  1. Protease inhibitors, a variety of proteases like trypsin, thrombin, kallikrein and plasmin
  2. Largest non-lg plasma protein (800,000 D)
  3. Synthesized by the liver
  4. A major component of A2-globulin fraction
A

Alpha 2-macroglobulin

83
Q

Reference Value for Alpha 2-macroglobulin

A

18-45 mg/dl

84
Q
  1. Synthesized by the liver
  2. 2 molecules of Ferric iron bind reversibly by preventing iron deposition in tissue
  3. Amajor component of the beta globulin fraction
  4. Negative Acute Phase Reactant
A

Transferrin (Siderophilin)

85
Q
  1. Natural defense and enhanced immune response by cell lysis
  2. Synthesize by the liver
A

Complement

86
Q

most abundant complement protein in human serum

87
Q

second most abundant

88
Q

Reference range for complement

A

30-75 U/ml

89
Q
  1. precursor of a fibrin clot, elevate with other acute phase reactants
  2. one of the largest proteins in plasma
  3. classified as a glycoprotein
  4. normally seen between beta-gamma region in electrophoresis
A

Fibrinogen

90
Q

Reference range for fibrinogen

A

200-400 mg/dl

91
Q
  1. Synthesized by the liver
  2. A small beta globulin that binds to free heme
  3. used to measure/diagnose hemolytic uremic syndrome
  4. acute phase reactant
92
Q

Transports lipids (VLDL)

A

Pre-B-lipoprotein

93
Q

Transports lipids (LDL)

A

B-lipoprotein

94
Q

Transports lipids (LDL)

A

B-lipoprotein

95
Q
  1. Single polypeptide chain that is a component of the light chain of HLA class I
  2. Freely filtered by the glomerulus and completely reabsorbed
A

B2- microglobulin

96
Q
  1. APR promotes phagocytosis
  2. Cardiac marker and inflammatory marker
A

C-reactive protein

97
Q

glycoproteins produced by plasma B cells

A

Immunoglobulins

98
Q

is most abundant antibody in plasma and lymph

99
Q

is the main antibody in mucous secretion

100
Q

is the first antibody that appears in response to antigenic stimulation

101
Q

is the antibody for allergic and anaphylactic reactions

102
Q

is present mostly on the surface of B cells

103
Q
  1. Type of cancer that develops from plasma cells in the bone marrow
  2. Increased plasma cells
  3. Elevated Total Protein
  4. Elevated serum creatinine
  5. Increased ionized calcium
  6. Urine: (+ ) Bence Jones Protein
  7. Electrophoretic pattern: Presence of a shape peak in the gamma globulin region
A

MULTIPLE MYELOMA

104
Q
  1. An autoimmune disorder in which the body attacks itself by mistake
  2. Presence of oligoclonal banding
  3. Demyelination
  4. Increased myelin basic protein
A

MULTIPLE SCLEROSIS

Clinical Chemistry-MIDTERMS (8 decks)

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