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MLT 203 > Proteins > Flashcards

Proteins Flashcards

1
Q

Protein definition

A

Substances made of amino acids.

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2
Q

Peptide

A

When two or more amino acids join

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3
Q

Elements in proteins

A

Carbon, Hydrogen, Oxygen, Nitrogen, Sulfur

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4
Q

Nitrogen in proteins

A

16%
This content allows us to differentiate between proteins and other substances
Used to measure total protein

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5
Q

Amino acids

A
  • Building blocks of proteins
  • chemical properties determine biological function
  • synthesized in body or ingested
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6
Q

MILL PATH TV (essential amino acids)

A 
Methionine
Isoleucine
Leucine
Lysine
Phenylalanine 
Arginine (semi)
Tryptophan
Histidine
Threonine
Valine
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7
Q

R group

A

Area of structure that differentiates amino acids

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8
Q

Glycine

A

Smallest and simplest amino acid

  • used as sweetener
  • used as sleep aid
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9
Q

Peptide bond

A

Formed when molecule of water removed from two amino acids

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10
Q

Peptide bond (biruet)

A

Used to measure total protein

-color is proportional to number of bonds)

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11
Q

Amino acids structure

A 
Amino group (N) (Base) 
Carboxyl (C) (Acid) 
R group (function)
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12
Q

Protein in serum (amino acid #)

A

100-150 amino acids

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13
Q

Amphoteric

A

Containing two ionizable sites

can serve as acid or base to provide buffering capacity to body

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14
Q

Proton accepting group

A

NH2

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15
Q

Proton donating group

A

COOH

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16
Q

Proton donating group

A

COOH

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17
Q

Buffering capacity of proteins

A

Comes from terminal groups

allow amino acid to pick up or release H+

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18
Q

Protein in alkaline solution

A

Amino acid acts as an acid and releases H+

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19
Q

Protein in acidic solution

A

Amino. acid acts as a base and absorbs H+

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20
Q

Isoelectric point (pI)

A

pH at which the amino acid or protein has no net charge

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21
Q

protein pH range

A

5.5-8.0

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22
Q

pH > pI

A

net negative charge

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23
Q

pH < pI

A

net positive charge

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24
Q

Primary structure

A

Number and types of amino acids in protein

“beads on string”

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25
Q

sickle cell disease

A

Valine is substituted for glutamic acid in hgb A (forms hgb S)

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26
Q

secondary structure

A

regularly repeating structures stabilized by hydrogen bonds

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27
Q

secondary structure (3 types)

A

alpha-helix
beta-pleated sheets
random coils

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28
Q

tertiary structure

A

overall shape/conformation
-folding of R-groups of other amino acids
determines function

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29
Q

quarternary structure

A

two or more polypeptide chains to form a protein

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30
Q

ex of quarternary structure

A

Hemoglobin

  • 4 polypeptide chains
  • CK
  • iron containing heme groups
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31
Q

denaturation

A

disruption of native folded structure of protein. disrupts function of protein

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32
Q

causes of denaturation

A
  • heat
  • change in pH
  • mechanical
  • chemicals
  • enzymatic activity
  • UV light
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33
Q

globular proteins

A
  • compact, coiled, tightly folded
  • soluble in water
  • transporters, enzymes, messengers
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34
Q

globular protein examples

A
  • albumin
  • hemoglobin
  • immunoglobulines
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35
Q

fibrous proteins

A
  • form long protein filaments (asymetrical)
  • insoluble (R groups)
  • tendons, bones, muscle
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36
Q

fibrous protein examples

A
  • collagen, elastin
  • keratin
  • fibrin
  • myosin
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37
Q

conjugated proteins

A

consist of protein and nonprotein (prosthetic) groups.

metalloprotein, lipoprotein, glyco, muco, nucleo…etc

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38
Q

metalloproteins

A

metal ion attached

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39
Q

metalloprotein examples

A

ferritin (Fe)
ceruloplasmin (Cu)
Hemoglobin (complex metal)

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40
Q

Lipoproteins

A

lipids and proteins

-HDL, VLDL, cholesterol, triglycerides

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41
Q

glycoproteins

A

-sugar group attached

simple protein and carbohydrates

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42
Q

glycoprotein examples

A
  • haptoglobin

- a1-antitrypsin

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43
Q

mucoproteins

A

large, complex carbohydrates

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44
Q

mucoprotein example

A

mucin

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45
Q

nucleoprotein

A

simple protein and nucleic acids (RNA, DNA)

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46
Q

nucleoprotein example

A

chromatin

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47
Q

protein metabolism location

A

originates in digestive tract

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48
Q

protein metabolism process

A

amino acids are absorbed from intestines into blood, become part of amino acid pool in body.
insufficient quantities can limit synthesis and lower levels of essential proteins

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49
Q

nitrogen storage

A

no designated storage depots in body

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50
Q

healthy nitrogen balance

A

intake and excretion are equal

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51
Q

positive nitrogen balance

A

intake exceeds loss

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52
Q

who has positive nitrogen balance

A

pregnant women, children, adults recovering from illness

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53
Q

negative nitrogen balance

A

loss exceeds intake

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54
Q

who has negative nitrogen balance

A

excessive tissue destruction; burns, wasting disease, high fevers or starvation

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55
Q

protein synthesis location

A

synthesized in liver with exceptions

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56
Q

protein synthesis exceptions

A

immunoglobulins
hemoglobin
protein hormones
coagulation factors

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57
Q

enzyme funciton

A

catalyze chemical reactions

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58
Q

enzyme examples

A
  • transaminases
  • dehydrogenases
  • phosphates
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59
Q

hormone function

A

messengers that control actions of specific cells or organs

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60
Q

hormone examples

A

insulin, growth hormone, cortisol

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61
Q

transport hormone function

A

transport ions and molecules across biological membranes

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62
Q

transport hormone examples

A

hemoglobin, albumin, transferrin

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63
Q

immunoglobulin function

A

mediate humoral response to identify and neutralize foreign invaders

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64
Q

immunoglobulin examples

A

IgG, IgM, IgA

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65
Q

structural protein function

A

structure of cells and tissues

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66
Q

structural protein examples

A

collagen, elastin, keratin

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67
Q

storage protein function

A

reserves of metal ions and amino acids

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68
Q

storage protein example

A

ferritin (stores Fe)

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69
Q

energy protein

A

reserve source of energy

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70
Q

osmotic force proteins

A

maintain water distribution between cells and tissue, interstitial compartments and vasculature

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71
Q

osmotic force protein example

A

albumin

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72
Q

how proteins maintain osmotic pressure

A

proteins don’t cross capillary membranes. water is absorbed into venous space.
if protein content is low, more water can pass through membrane and osmotic pressure will be low

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73
Q

result of low osmotic pressure

A

edema

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74
Q

aminoacidopathies

A

rare

enzyme defect that inhibits body’s ability to metabolize certain amino acids

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75
Q

aminoacidopathy abnormalities

A

problem with enzyme activity

membrane transport system for amino acids

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76
Q

result of aminoacidopathies

A

buildup of toxic amino acids

byproducts of amino acid metabolism in blood

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77
Q

IEM

A

inborn error of metabolism (metabolic defects from birth)

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78
Q

why do we not care about IEM in utero

A

mom’s system will make up for any error in metabolism

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79
Q

PKU

A

-IEM
absence of deficiency of phenylalanine hydroxylate
-increased formation of phenylalanine metabolites

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80
Q

PKU dietary restrictions

A

meat, fish, nuts, dairy

calculated amounts of cereal, starch, fruit, veg, milk substitutes

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81
Q

result of PKU

A

build up of phenylpyruvic acid

-decreased tyrosine

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82
Q

enzyme deficiency in PKU

A

phenylalanine hydroxylase

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83
Q

Tyrosinemia

A

accumulation of excess tyrosine in the plasma producing urine overflow

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84
Q

tyrosinemia urine

A

excess tyrosine or degredation products

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85
Q

tyrosinemia smell

A

boiled cabbage

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86
Q

tyrosinemia enzyme deficiency

A

tyrosine transaminase

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87
Q

tyrosinemia types

A

type 1, type 2, type 3

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88
Q

Alkaptonuria enzyme

A

homegentisic acid oxidase

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89
Q

alkaptonuria urine

A

black urine, dark

alkaline

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90
Q

homogentisic acid oxidase

A

used i ncatabolism of phenyalanine and tyrosine

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91
Q

adult alkaptonuria

A

ochronosis, alkaline urine, arthritis, liver, cardiac disorders

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92
Q

maple syrup urine disease

A

thick, dark, sweet urine

elevated valine, leucine, isoleucine

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93
Q

MSUD enzyme

A

branched chain keto acid decarboxylase

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94
Q

maple syrup urine disease diagnosis

A

within 11 days of live, or else severe intellectual disability

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95
Q

cystinuria

A

elevated cystine in urine
defect in renal tubular reabsorption of cystine
(not an enzyme deficiency)

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96
Q

two modes of cystinuria

A
  • reabsorption of all 4 amino acids (cystine, lysine, arginine, ornithine) is affected
  • reabsorption of cystine and lysine
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97
Q

cystinuria result

A

kidney stones and crystals

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98
Q

cystinosis

A

inherited lysosomal storage disease resulting in cystine deposits in lysosome cells throughout the body

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99
Q

homocystinuria

A

autosomal IEM

defective metabolism of methionine

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100
Q

homocystinura result

A

failure to thrive, thrombosis, death

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101
Q

PKU markers

A

mousy odor

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102
Q

Amino acid analysis

A

evaluated patients with IEM

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103
Q

amino acid specimen collection

A 
draw 6-8 hour fast (avoid dietary proteins)
heparine tube 
remove plasma
avoid WBC and hemolysis
Perform immediately or freeze 
-can use urine, chromatography
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104
Q

acute phase reactants

A

rapid and coordinated change/response

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105
Q

acute phase reactants intiation

A

intiated by tissue damage

-infection, inflammation, RA, trauma, burns

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106
Q

negative acute phase reactant

A

proteins will decrease

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107
Q

positive acute phase reactants

A

proteins will increase

108
Q

acute phase reactant protein

A

proteins needed to deal with tissue damage will be generated, whereas other proteins will be inhibited

109
Q

prealbumin

A

TTR

migrates ahead of albumin in protein electrophoresis

110
Q

prealbumin visibility

A

not visible in low concentration

111
Q

prealbumin job

A

transport thyroid hormones, retinol (vitamin A)

112
Q

negative acute phase proteins

A

prealbumin
albumin
transferrin

113
Q

where is prealbumin made

A

liver

114
Q

increased prealbumin

A

steroids, alcoholism, chronic renal failure

115
Q

decreased prealbumin

A

hepatic damage
acute phase inflammatory response
tissue necrosis
poor nutrition

116
Q

PEM

A

protein energy malnutrition

sensitive marker of poor nutritional status

117
Q

prealbumin reference range

A

195-350 mg/dl

118
Q

albumin synthezised where

A

synthesized in liver

119
Q

albumin amount in plasma

A

protein present in highest concentration in the plasma 60%

120
Q

albumin functions

A
  • maintenance of colloid osmotic pressure
  • buffer pH
  • negatively charged, acts as magnet for water (pulls into vascularature)
  • negative acute phase protein
  • transport various molecules (bilirubin, meds, hormones)
121
Q

albumin reference range

A

3.5-5.0 mg/dl

122
Q

increased albumin

A

hyperalbuminemia

dehydration
steroids
excessive albumin infusions

123
Q

decreased albumin

A 
hypoalbuminemia
liver disease
malabsorption
diarrhea
renal disease
inflammation
dilution by polydipsia/IV fluids
124
Q

makes up 90% of alpha 1 proteins

A

a1 antitrypsin

125
Q

a1 antitrypsin

A

acute phase reactant

inflammatory response.

126
Q

decreased a1 antitrysin

A

emphysema, congential cirrhosis

127
Q

increased a1 antitrysin

A

inflammatory reactions, contraceptive use

128
Q

main fetal protein

A

alpha fetoprotein (AFP)

129
Q

a1 antitrysin synthesis

A

in liver

130
Q

no a1 antitrypsin present

A

emphysema.

131
Q

job of a1 antitrypsin

A

cleans byproducts of macrophages in lungs

132
Q

excess AFP

A

spina bifida, neural tube issue

133
Q

AFP decreased

A

down syndrome

134
Q

haptoglobulin

A

acute phase reactant
binds hemoglobin
indicator of hemolysis

135
Q

increased haptoglobulin

A

inflammatory disease
RA
burns
nephrotic syndrome

136
Q

decreased haptoglobulin

A

hemolytic anemia

liver disease

137
Q

a1 globulins

A

AFP
a1 antitrypsin
a1 acid glycoprotein

138
Q

why we want to bind free hemoglobin

A

hemoglobin can be oxidized into a free radicals

139
Q

a2 globulins

A

haptoglobin
cerruloplasmin
a2 macroglobulin

140
Q

cerruloplasmin function

A

acute phase reactant

binds 90% of copper

141
Q

increased cerruloplasmin

A

inflammation
infection
pregnancy
tissue damage

142
Q

decreased cerruloplasmin

A

malnutrition
liver disease
wilson’s disease
(copper deposits throughout body especially eyes)

143
Q

a2 macroglobulin function

A

acute phase reactant
protease inhibitor, trysin, pepsin, plasmin
associated with coag cascade

144
Q

increased a2 macroglobulin

A
  • nephrotic syndrom
  • oral contraceptives
  • hormone replacement
145
Q

decreased a2 macroglobulin

A

pancreatitis

advanced prostate cancer

146
Q

beta globulins

A 
transferrins
hemopexin
B-lipoproteins
B-microglobulin
fibrinogen
complement
CRP
147
Q

transferrin function

A

transport iron
prevent iron loss
negative acute phase reactant

148
Q

increased transferrin

A
  • iron deficiency
  • anemia
  • hepatitis
  • pregnancy
  • HRT
149
Q

decreased transferrin

A
  • inflammation
  • malignancy
  • nephrotic syndrome
  • malnutrition
  • marker of PEM
150
Q

hemopexin function

A

binds free heme

151
Q

increased hemopexin

A
  • inflammation
  • diabetes
  • melanoma
  • pregnancy
152
Q

decreased hemopexin

A

-hemolytic anemia (hemopexin is used up)

153
Q

b-lipoprotein function

A

transport lipids

154
Q

increased b-lipoproteins

A
  • heart disease
  • athreosclerosis
  • diabetes
  • hypothyroidism
155
Q

decreased b-lipoproteins

A

malnutrition

156
Q

b-microglobulin function

A

component of immune system

-HLA molecules (blood matching for donation)

157
Q

increased b-microglobulin

A
  • RA
  • lupus
  • renal failure
158
Q

fibrinogen function

A
  • forms a fibrin clot when activated by thrombin

- acute phase reactant

159
Q

increased fibrinogen

A

pregnancy, oral conctraceptive

160
Q

decreased fibirnogen

A

excessive coagulation

161
Q

complement function

A

immune response

acute phase reaction

162
Q

increased complement

A

inflammation

163
Q

decreased complement

A

malnutrition

hemolytic anemima

164
Q

CRP function

A

acute phase reactant

165
Q

increased CRP

A

tissue necrosis
cardiac disease
bacterial infection
RA

166
Q

high snesitivity, low specificity

A

CRP testing

167
Q

immunoglobulin structure

A

heavy chain
antigen binding site
disulfide bonds
carbohydrate side chains

168
Q

immunoglobulin synthesis

A

mature B cells in plasma

169
Q

majority of protein synthesis

A

liver

170
Q

y globulins

A
  • IgG
  • IgA
  • IgM
  • IgD
  • IgE
171
Q

majority of immunolgobuin

A

IgG

172
Q

IgG function

A

antibodies

173
Q

increased IgG

A
  • liver disease
  • infection
  • parasitic disease
  • RA
174
Q

decreased immunoglobins

A

immunodeficiency disorders

175
Q

IgA function

A

antibodies in secretion

ex. colostrum

176
Q

increased IgA

A
  • liver disease
  • infection
  • autoimmune disease
177
Q

decreased IgA

A

depressed protein synthesis

178
Q

largets immunoglobulin

A

IgM

179
Q

IgM function

A

early response antibodies

180
Q

increased IgM

A

toxicoplasmosis

181
Q

decreased IgM

A

hereditary

182
Q

IgD fucntion

A

antibodies

183
Q

increased IgD

A

infection
liver desase
connective tissue disorders

184
Q

IgE function

A

allergy antibodies

185
Q

increased IgE

A

not diagnostic
inflammatory disease
allergens

186
Q

myoglobin

A

found in skeletal/cardiac muscle

187
Q

myoglobin function

A

carry oxygen to muscles

188
Q

myoglobin and tropronin

A

used to help rule out MI

189
Q

troponin

A

cardiac biomarker

190
Q

increased myoglobin

A

muscle disease, crush injuries

191
Q

myglobin size

A

can pass through the nephron and damage kidney

192
Q

brain natriuretic peptide (BNP) function

A

fluid homeostasis

distinguishes AMI and CHF

193
Q

fetal fibronectin

A

used to help predict short term delivery risk of premature delivery

194
Q

total protein reference range

A

6.5-8.3 mg/dl

195
Q

lower total protein

A 
hospital patients (0.5 lower)
age (decline)
196
Q

artificial increased total protein

A

increased tourniquet application (by 0.5 mg/dl)

197
Q

hyperproteinemia ref range

A

total protein over 8.3 mg/dl

198
Q

causes of hyperproteinemia

A

-dehydration –> decreased water = increased protein
(vomiting, diarrhea, diabetes)
-excess gamma globulins
(multiple myeloma, waldestron’s)

199
Q

hypoproteinemia ref range

A

total protein <6.5 mg/dl

200
Q

negative nitrogen balance

A

hypoproteinemia

201
Q

causes of hypoproteinemia

A
  • excessive loss (renal disease)
  • decreased intake
  • decreased synthesis (liver disease)
  • acceleration of protein catabolism
202
Q

A/G ratio equation

A

(calc. globulin)= (total protein)-(albumin)

203
Q

A/G ratio reference range

A

1.0-1.8

204
Q

low AG ratio

A
  • overproduction of globulins

- decreased albumin

205
Q

high AG ratio

A

-underproduction of globulins

206
Q

fibrinogen tube and specimen

A

green top: plasma

207
Q

(Protein methodology) Kjedahl method principle

A

Digestion of protein, measurement of nitrogen content

-assume nitrogen content is 16%

208
Q

Refractometry (total protein)

A

Measurement of refractive index due to solutes in the serum

-assume nonprotein solids are in same concentration as the serum

209
Q

Biuret (tot protein) principle

A

Formation of violet-colored compound chelate between Cu2- ions (cupric) and peptide bonds.
more peptide bonds = more color

210
Q

Biuret method specimen

A

serum or plasma

211
Q

Biuret wavelength

A

450 nm

212
Q

Spectrophotometer interference

A

lipids, icteric, hemolysis

213
Q

Biuret requirements

A

2 peptide bonds

alkaline medium

214
Q

Dye binding (tot prot)

A

Protein binds to dye and causes spectral shift in the absorbance (465 nm-595nm)

215
Q

Dye binding (tot protein) notes

A

unequal dye requires caution

216
Q

Biuret method advantages

A

simple,automated,precise

217
Q

biuret method disadvantages

A

hemolysis can elevate RBC proteins.

lipemia, biirubinemia, turbidity

218
Q

Bromcresol green (albumin dye binding) principle

A

Albumin binds to dye, causes shift in absorbance
not as specific for albumin
most common

219
Q

Bromcresol purple (albumin dying)

A

Albumin binds to dye

Specific, sensitive, precise

220
Q

serum protein electrophoresis clinical application

A

when tissues responsible for synthesis or clearance of proteins are altered by disease, serum reveals patterns helpful for diagnosis

221
Q

how serum protein electrophoresis separates

A

Basis of electric charge densities

222
Q

fastest migrating protein

A

albumin

223
Q

intermediate migrating protein

A

alpha1, alpha 2, beta-globulins

224
Q

slowest migrating protein

A

gamma globulines

225
Q

electrophoresis process

A

migrate on agarose gel, fix proteins, stain for scanning

226
Q

pH buffer for serum protein electrophoresis

A

pH 8.6

227
Q

why SPE is performed on serum

A

fibrinogen is absent

228
Q

rate of migration depends on

A 
Net electrical charge
pH buffer
pI mobility
size/shape
electrical field
supporting medium
temperature
229
Q

isoelectric point of a protein and pH

A

if pH is greater than pI, specimen will move towards anodes

230
Q

densitometry dyes

A

Ponceau S, Amido black, Coomaise blue

231
Q

Densitometry protein strips

A

gel bands are dyed, and passed through optical beam and absorbance is read

232
Q

densitometry wavelength

A

520-640 nm depending on stain

233
Q

densitometry peaks

A

more protein = darker bands

234
Q

abbie ____ is attracted to Andy ____ because of his _____ attitude

A

albumin, anode, positive

235
Q

why is serum electrophoresis

A

to see if there is a presence of abnormal proteins, or absence of normal proteins

236
Q

densitometry equation

A

relative %=(absorb. apecific band/absorb. all bands) X 100

237
Q

greater the concentration =

A

higher the absorbance

238
Q

densitometry absolute concentration

A

(Relative % of each band) X (Total serum protein)

239
Q

albumin band

A

dark, tight band

240
Q

gamma globulin bands

A

many immunoglobulins with different charges

lighter wider band, short peak

241
Q

albumin relative % (ref range)

A

53-65

242
Q

albumin absolute concentration (ref range)

A

3.5-5.0 g/dl

243
Q

a1 globulin relative % ref range

A

2-5%

244
Q

a1 globulin absolute conc. ref range

A

0.1-0.3 g/dl

245
Q

a2-globulin % reference range

A

7-13%

246
Q

a2-globulin absolute conc. ref reange

A

0.6-1.0

247
Q

B-globulin % ref range

A

8-14%

248
Q

B-globulin absolute conc. ref range

A

0.7-1.1 g/dl

249
Q

y-globulin % ref range

A

12-20%

250
Q

y-globulin absolute conc. ref range

A

0.8-1.6 g/dl

251
Q

nephrotic syndrome (protein)

A

protein lost from blood to urine. (damage to kidney)

decreased albumin, increased a2, B-globulins

252
Q

nephrotic syndrome symptoms

A 
edema 
blood clots
high cholesterol
foamy urine
fatty/waxy casts
253
Q

edema and protein

A

when albumin leaves through urine, water cannot pass through into vasculature and accumulates into extravascular space

254
Q

y-globulin increase

A

-immune reaction
-RA
-cirrhosis
-liver disease
metastatic cancer
-bacterial infection

255
Q

y-globulin decrease

A
  • immune deficiency
  • manifest in infancy
  • monoclonal gammopathy
  • immunosuppresive therapy
256
Q

monoclonal increase

A
  • excessive production of single immunoglobulin by single plasma line
  • appears as distinct band
  • requires further investigation
257
Q

IgM overproduction

A

Waldenstroms Macroglobulinemia

258
Q

overproduction of any single immunoglobulin

A

Multiple myeloma

259
Q

bence jones protein

A

overproduction of light chains on immunoglobulins

260
Q

monclonal

A

one type of protein

261
Q

polyclonal

A

multiple types of proteins

262
Q

diffused band

A

polyclonal

263
Q

cirrhosis

A

polyclonal increase in y-proteins

-increased IgA

264
Q

fusion of Beta and gamma bands

A

“bridging”
occurs in cirrhosis
fast moving gamma prevent resolution of beta

265
Q

hypogammaglobulinemia

A

low gamma globulins due to reduced antibodies

  • immunocompromised
  • staining erro

MLT 203 (10 decks)

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