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Chemistry! > Amino Acids > Flashcards

Amino Acids Flashcards

1
Q

What is the functional structure of amino acids

A

They’re simple, organic compounds that are the building blocks for proteins. They contain one amino group (N-terminal) and one carboxyl group (C-terminal), and are linked together with peptide bonds

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2
Q

Absorption of amino acids takes place where? Where do dietary proteins and amino acids not absorbed take place?

A

Absorption takes place in the small intestines into the bloodstream.

The ones that do not are excreted in feces

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3
Q

What are essential amino acids and which ones are they?

A

they’re the amino acids that cannot be synthesized in vivo fast enough and must be acquired by diet.

  • histidine
  • isoleucine
  • leucine
  • methionine
  • phenylalanine
  • theonine
  • tryptophan
  • valine
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4
Q

what are non-essential amino acids and which ones are they?

A

the body can synthesize adequate amounts of these, so dietary intake isn’t necessary

  • alanine
  • asparagine
  • aspartic acid
  • glutamic acid
  • selenocysteine
  • serine
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5
Q

Gastrin stimulates the secretion of what two things to promote the denaturation of proteins?

A

HCl (hydrochloric acid) and pepsin

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6
Q

Proteins catalyze almost all reactions in living cells. What are five of their functions?

A
  • biochemical reactions
  • transporting metals
  • acting as receptors for hormones
  • providing structure and support
  • being part of the immune response
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7
Q

What causes maple syrup urine disease? What are some of the symptoms?

A

deficiency in branched chain keto acid decarboxylase. Leads to excess branched chain amino acids (valine, leucine, and isoleucine), which causes metabolic acidosis

maple syrup odor urine, seizures, coma, death

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8
Q

phenylketonuria is caused by what? What are some symptoms?

A

inability to metabolize phenylalanine
- this test is done on newborns

mousy odor urine, cerebral development loss, loss of interest, mental retardation, restlessness, and irritability

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9
Q

What causes cystinuria and what are some symptoms?

A

defect in renal tubule transport protein affecting dibasic amino acids

causes cystine kidney stones and crystalluria

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10
Q

what causes alkaptonuria and what are the symptoms?

A

inability to properly degrade tyrosine/defect in homogentistic acid

black urine and black cartilage and arthritis

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11
Q

What are parameters to be met when testing amino acids?

A

-blood samples after a fast
- heparin tube (Plasma removed)
- perform immediately or freeze at -40ºC
- urinary amino acid testing can be performed on random samples
- thin-layer chromatography

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12
Q

What are the five elements that make up protein structure? What are the four levels of protein structure?

A

Carbon, oxygen, hydrogen, nitrogen, and sulfur

  • primary: number, type, and sequence of aa in a polypeptide chain
  • secondary: commonly formed arrangements (alpha-helix and beta-pleated sheets) stabilized by hydrogen bonds between amino acids
  • tertiary: the overall shape or conformation of the protein molecule
  • quaternary: the interactions of one or more protein molecule (subunit) to function as a single unit (multimer)
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13
Q

What part of the protein changes the property of the protein? What determines if the protein is negatively or positively charged?

A

amino acid side chain (R group) changes the protein properties. Proteins are pos or neg charged due to the N- or C- terminal ends

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14
Q

What are the two protein groups that are not involved in the peptide bond/can exist in different charged forms depending on the pH of the surrounding environment? What happens when the pH of a solution increases?

A

the acid or base groups

as pH goes up,
- carboxyl groups become carboxylate
- ammonium groups to amino groups

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15
Q

What is the isoelectric point, and what happens when the pH increases or decreases from it?

A

isoelectric point: pH at which amino acid or protein has NO net charge
- pH greater than isoelectric point: net neg charge
- pH less than isoelectric point: net pos charge

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16
Q

Where are plasma proteins synthesized before being excreted into circulation? What is amino acids sequence determined by?

A

protein synthesis occurs in the liver

aa sequence determined by corresponding sequence of nitrogen bases of DNA (three-nucleotide combination = codon)

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17
Q

what is transcription and translation of protein synthesis?

A

transcription: formation of complementary strands of mRNA in the nucleus to be used as a template

translation: moving the mRNA across the nuclear membrane to the cytoplasm; then the mRNA strand threaded into the ribosome provided the RNA sequence for the codons with their corresponding aa’s to form a polypeptide chain

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18
Q

Proteins have no designated storage. They are repeatedly _____ and then _______. What is maintained by equal intake and excretion of amino acids? What happens when there is too much or too little of this substance?

A

they’re repeatedly synthesized and then degraded

Nitrogen balance is maintained by aa intake and excretion

Too little nitrogen: excessive tissue destruction, burns, starvation
Too much nitrogen: aa converted to urea for kidney excretion and into glucose or ketones for energy

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19
Q

Classification of proteins depend on what three things? What two classes (and subclasses) of proteins are there?

A

based on structure, composition, and function

  1. simple proteins: upon hydrolysis, yield only amino acids (eg albumin and troponin)
  2. conjugated/complex proteins: composed of a protein and a non-protein moiety
    - enzymes, hormones, immunoglobulins
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20
Q

Routine analysis measurement of protein includes what three parts? What are three functions of plasma proteins?

A

measurement of total protein, albumin, and A/G (albumin/globulin) ratio

functions: catabolism, nitrogen balance, and hormone regulator

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21
Q

What is prealbumin, what is it a marker for in CSF, and what do increased and decreased concentrations indicate?

A

transport protein for thyroid hormones T3 and T4 (thyroxine and triiodothyronine).

Forms a complex with retinol-binding protein to transport vitamin A in CSF

Marker for nasal discharge
- decreased: hepatic damage, tissue necrosis, and poor nutrition
- increased: steroid therapy, alcohol abuse, and chronic renal failure

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22
Q

What is the roles of albumin?

A

maintains homeostatic pH by serving as a buffer in circulation and maintains the fluid balance between extra- and intra-vascular spaces (colloid osmotic pressure). It also binds bilirubin

negative acute phase protein

most abundant in plasma

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23
Q

what do increased and decreased concentrations of albumin indicate?

A

increased: not usually significant, but can mean dehydration

decreased: acute inflammatory response, liver/kidney disease, malabsorption/nutrition

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24
Q

What is the function of alpha-1-antitrypsin (A1AT), what kind of globulin is it, and what do increases and decreases of it signify?

A

positive acute phase reactant glycoprotein that functions to inhibit neutrophil elastase
-it’s a major protease inhibitor

it’s a alpha-1-globulin

increase: inflammation, pregnancy, contraceptive use

decrease: lung damage, emphysema

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25
Q

What is the function of alpha-2-macroglobulin, what kind of globulin is it, and what is the significance of its increase and decrease?

A

it’s an alpha-2-globulin that acts as a protease inhibitor (eg for insulin and pepsin)

regulates growth factors and cytokines

increased in:
- nephrotic syndrome due to its size, pregnancy, renal disease (secondary to diabetes mellitus)
decreased in:
- pancreatitis and liver disease

associated w/Alzheimer’s

26
Q

Where is alpha-1 fetoprotein made, what kind of globulin is it, and what are is the significance of its increase or decrease?

A

it’s an alpha-1 globulin made in utero

increase: inflammation, increased risk of spina bifida, neural tube defects, and general fetal distress

decrease: risk marker for Down syndrome

27
Q

What is the function of alpha-1 glycoprotein and what is the significance of its increase?

A

it maintains the barrier function of capillaries, regulates immunity, and binds endogenous/exogenous substances

made mostly from carbs

increase: stress, inflammation, tissue damage, AMI, trauma, pregnancy, cancer, pneumonia, RA and surgery

28
Q

What is the function of haptoglobin, what kind of globulin is it, and what is the significance of its increase and decrease?

A

An alpha-2 globulin that binds to free Hgb to prevent the loss of iron in the urine. Used to evaluate primary hemolytic anemias, and aids in distinguishing intra from extravascular hemolysis

increase: inflammation, ulcerative colitis, acute rheumatic disease, AMI, and severe infection

decrease: hemolytic anemia and decreased liver synthesis

29
Q

What is the function of ceruloplasmin, what kind of glycoprotein is it, and what is the significance of its increase and decrease?

A

An alpha-2 glycoprotein that transports copper and is measure in blood and urine to diagnose Wilson’s disease (AR disorder)

increased: inflammation, infection, tissue damage, some cancers, pregnancy, estrogen ingestion / oral contraceptives

decreased: Wilson’s disease (with Kayser Fletcher rings in eyes), malnutrition/malabsorption, severe liver disease, nephrotic syndrome, Menke’s syndrome (decrease copper adsorption)

30
Q

What is the function of transferrin, what kind of globulin is it, and what is the significance of its increase or decrease?

A

it’s a beta globulin, negative acute phase reactant, and binds iron to and from storage

increase: IDA (due to the body trying to compensate for loss of iron)

decrease: liver disease, insufficient intake of proteins, nephrotic syndrome (it’s lost through the kidneys)

31
Q

What is beta-2 microglobulin, and what is the significance of its increase?

A

it’s the light chain component of the MHC or HLA, and found in high concentrations on lymphs

increased in plasma:
- impaired renal clearance or overproduction (due to inflammatory diseases like SLE)
- in HIV: high B2M in absence of renal failure means large lymph turnover rate

increased in urine:
- renal tubular damage/disease

32
Q

What is the function of fibrinogen, what kind of globulin is it, where should you not find it, and what is the significance of its increase and decrease?

A

It’s a beta globulin, one of the largest proteins in the blood plasma, and functions to form a fibrin clot when activated by thrombin.

Shouldn’t see it in serum

increase: inflammation, pregnancy and oral contraceptives

decrease: excessive coagulation and fibrinogen disorders (a/ hypofibrinogenemia)

33
Q

What is C-reactive protein, what kind of globulin is it, and what are conditions related to its increase?

A

It’s a beta-globulin that is one of the first acute-phase reactant to rise in response to inflammatory disease. hs-CRPLevels help determine risk of cardiovascular disease.

increase: SLE or RA, rheumatic fever, bacterial/viral infection, gout, active coagulation, and atherosclerosis (which activates complement)

(CRP over 1 mg/dL is considered high)

34
Q

What is the main complement protein, what kind of globulin is complement, and what is the significance of its increase and decrease?

A

C3 is a beta globulin

increase: inflammation

decrease: malnutrition, SLE, and intravascular coagulopathies (DIC)

35
Q

Immunoglobulin structure types, classes, function, and what kind of globulin are the immunoglobulins?

A

Structure can be: monomer (IgG/D/E), dimer (IgA) or pentamer (IgM)

Immunoglobulins are gamma globulins made from two identical light chains (kappa and lambda) and two identical heavy chains (the Ig classes)

36
Q

What are special characteristics of IgG, and what do increases and decreases of it mean?

A

Most abundant Ig

second responder to bacteria, fungus, and viruses by agglutination, opsonization, and complement activation and neutralizing toxins

can cross the placenta

increased: liver disease/autoimmune disease

deceased: acquired immunodeficiency and increased susceptibility to infections

37
Q

What are the special characteristics of IgA, and what is the significance of its increase and decrease?

A

main Ig found in mucous secretions (eg tears, saliva, vaginal fluid, respiratory/GI mucosa). Made by B lymphs.

Increase: liver disease, autoimmune disease, nutritional hepatic cirrhosis

Decrease: immunodeficiency and impaired protein synthesis

38
Q

What are the unique characteristics of IgM and what are the significances of its increase and decrease?

A

First Ig to appear in a antigenic stimulation, is a pentamer, only Ig made by the neonate

Increase: bacteria infections, toxoplasmosis, primary biliary cirrhosis, CMV, rubella/herpes

Decrease: hereditary immunodeficiencies, and protein-losing deficiencies

39
Q

Where are IgD found/made? What is the significance of its increase and decrease?

A

Present on the surface of most (but not all) B lymphs in their development. Most don’t get released into circulation

increase: infection, liver disease, and connective tissue disorders (SLE and RA)

40
Q

What is the significance of its increase and decrease of IgE

A

allergic and anaphylactic reactions, autoimmune processes, and parasitic infections

(circulation is low)

41
Q

What is troponin and its functions, as well as what is the significance of its increase?

A

three proteins that bind to filaments of striated skeletal muscle and cardiac muscle that are highly cardio-specific

gold standard measurement analyte for diagnosis of acute coronary syndromes
- Myocardial infarction, embolus, myocarditis, pericarditis, heart failure, intracranial insults, and sepsis

42
Q

What is beta-type natriuretic peptide?

A

A hormone released from ventricular walls due to hypertension and volume overload. It increases Na+ / water excretion, and vasodilation to lower blood pressure

Seen in patients with heart failure

43
Q

What is evaluated by total protein measurements, and what are the two main kinds of abnormal protein abnormalities?

A

Total protein measurements evaluates:
- nutritional status
- kidney disease
- liver disease

Hypoproteinemia and hyperproteinemia

44
Q

Hypoproteinemia is cause by?

A

excessive loss: renal disease, leakage into GI tract, blood loss, extensive burns

decreased synthesis: liver disease

increases protein catabolism: in burns, trauma, or other injuries

45
Q

hyperproteinemia is caused by?

A

dehydration:
- water loss in vessels while proteins remain in vessels
- vomiting, diarrhea, excessive sweating, diabetic acidosis, monoclonal protein production, and hypoaldosteronism

46
Q

What is Bence Jones protein, and what does it signify?

A

Bence Jones proteins are urine specific proteins (Ig light chains) in patients with plasma cell disorders:
- Multiple myeloma
- Waldenstrom’s macroglobulinemia

47
Q

What are three body fluids used to analyze serum proteins? What is electrophoresis, immunofixation, and immunoelectrophoresis?

A

urine, CSF, and serum

electrophoresis: separates proteins on the basis of their electric charge and density across agarose gel or cellulose acetate

immunoelectrophoresis: electrophoresis, and then antibodies are applied, diffuse onto a plate, and interact with patient antigens to make a line of precipitation

immunofix: insoluble antigen-antibody complexes (made with antiseras) that precipitate

48
Q

what is the order of protein electrophoresis migration (fastest to slowest) at a pH of 8.6?

A

Albumin, alpha-1 globulin, alpha-2 globulins, beta globulins, and gamma globulins

49
Q

Name the 3 alpha-1 globulins, 3 alpha-2 globulins, 5 beta globulins, and gamma globulins

A

alpha-1:
- alpha-1 antitrypsin
- alpha-1 fetoprotein
- alpha-1 glycoprotein

alpha-2:
- haptoglobin
- ceruloplasmin
- alpha-2 macroglobulin

beta:
- transferrin
- beta-2 microglobulin
- fibrinogen
- complement
- C-reactive protein

gamma: all immunoglobulins

50
Q

Nephrotic syndrome electrophoresis change from normal

A

decreased albumin, increased alpha-2, decreased gamma

51
Q

monoclonal gammopathy electrophoresis change from normal

A

sharp spike in gamma region

52
Q

hypogammaglobulinemia electrophoresis change from normal

A

flat gamma band

53
Q

liver disease/cirrhosis electrophoresis change from normal

A

decreased albumin and broad increase of gamma (beta-gamma bridging)

54
Q

acute inflammation / phase reaction electrophoresis change from normal

A

increased alpha-2 globulins (with a chance of decreased albumin)

55
Q

polyclonal gammopathy electrophoresis change from normal

A

broad increase of gamma globulins only

56
Q

what is the difference between hemoglobinopathies and thalassemias?

A

hemoglobinopathies: qualitative defects of Hgb

thalassemias: quantitative defects of Hgb

57
Q

what is the function of myoglobin, why don’t we use it as the main cardiac marker, and what is the significance of its increase?

A

carries oxygen from muscle cell membrane to mitochondria and serves as extra O2 reserve for longer exercise periods

Is the first cardiac marker to increase, but it decreases rapidly, so it’s not a good measure for heart conditions

increased in: striated muscle damage, myocardial infarction, rhabdomyolysis

58
Q

what are porphyrias?

A

mutations of the porphyrins (which are made in the synthesis of heme)

can be erythropoietic or hepatic, and therefore affect the liver or RBC production

59
Q

what does it mean that amino acids are amphoteric?

A

it means they have acidic and basic tendencies

60
Q

what are the two NEGATIVE acute phase reactants?

A

albumin

transferrin (beta globulin)

Chemistry! (9 decks)

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