Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

Clinical Chemistry Review > Amino Acids > Flashcards

Amino Acids Flashcards

(55 cards)

Start Studying
1
Q

amino acids

A

building blocks of proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

basic chemical structure of amino acid

A

one amino group and one carboxyl functional group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

alpha-carbon

A

N-terminal end and C-terminal end are bonded to this carbon.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

peptide bond

A

linkage of the amino group of one amino acid to the carboxyl group of another amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

polypeptide

A

chain of amino acids linked by peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

protein

A

large polypeptide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

size of proteins in serum

A

100-150 amino acids in length

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

essential amino acids- require dietary supplement

A

arginine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

nonessential amino acids-not required dietary supplement

A

alanine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine, and tyrosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

how much of total required daily energy do proteins provide

A

20%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what are the ketogenic amino acids

A

isoleucine, leucine, lysine, phenylalanine, tryptophan, tyrosine, and threonine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what are the glycogenic amino acids

A

alanine, arginine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, phenylalanine, tryptophan, tyrosine, and threonine, isoleucine, valine, histidine, proline, methionine,

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Role(s) of arginine

A

cell division, wound healing, stimulation of protein synthesis, immune function, release of hormones, and in conversion of ammonia to urea for excretion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Role(s) of histidine

A

grow and repair of body tissues, maintain myelin sheaths around nerve cells, precursor to histamine (immune response), manufacturing of red and white blood cells, protection from heavy metal toxicity, and source of carbon for synthesis of purine for DNA and RNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Role(s) of isoleucine, leucine, and valine

A

branched chain amino-acids; promote healing of muscle tissue, skin, and bones; regulation of blood glucose levels; maintain energy levels; isoleucine in hemoglobin formation; leucine in infant growth; leucine and valine in nitrogen balance in adults

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Role(s) of lysine

A

production of antibodies; lowering triglyceride levels; absorption and conservation of calcium; formation of collagen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Role(s) of methionine

A

initiation of translation of mRNA (first amino acid incorporated into N-terminal position of all amino acids); source of sulfur for metabolism and growth; breakdown of fats; detoxification of lead and other heavy metals; decrease muscle weakness and prevents brittle hair; reacts with ATP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Role(s) of phenylalanine

A

promotes alertness and vitality; elevates mood; decreases pain; aids in memory and learning; treatment for arthritis and depression; used by brain to produce norepinephrine; can interfere with serotonin production; direct precursor to tyrosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Role(s) of threonine

A

formation of collagen, elastin, and tooth enamel

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Role(s) of tryptophan

A

precursor for serotonin, melatonin, and niacin; natural relaxant; treatment of migrants, weight control, hyperactivity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Role(s) of alanine

A

product of DNA/dipeptide (anserine and carnosine) breakdown; transfers nitrogen from peripheral tissues to liver for processing and excretion; strengthens immune system through antibody production; reduces buildup of toxic substances when muscle protein is broken down quickly

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Role(s) of asparagine

A

derived from aspartic acid and ATP; transport of nitrogen; requisite amino acid for nervous system; synthesis of ammonia; conversion of amino acids through amination or transamination

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Role(s) of aspartic acid

Study These Flashcards
A

aka aspartate; precursor or asparagine, arginine, lysine, methionine, threonine, isoleucine; metabolite in citric acid cycle and urea cycle; participation in gluconeogenesis

24
Q

Role(s) of cysteine

Study These Flashcards
A

potentially toxic; absorbed as cystine; important structural and functional component of proteins

25
Role(s) of glutamic acid
aka glutamate; precursor to glutamine; neurotransmitter; dysregulation leads to epileptic seizures; metabolism of fats and sugars; transport of potassium in to spinal fluid
26
Role(s) of glutamine
precursor to proline; renal maintenance of acid-base balance; fuel for health digestive tract; basis of building blocks for synthesis or RNA and DNA; transport of ammonia to liver for metabolism
27
Role(s) of glycine
synthesis of nucleic acids, bile acids, proteins, peptides, purines, ATP, porphyrins, hemoglobin, glutathione, creatine, bile salts, glucose, glycogen, and other amino acids; detoxification of compounds in liver; inhibitory neurotransmitter in CNS; metal complexing agent; retards muscle degeneration
28
Role(s) of proline
precursor to hydroxyproline (needed for tendons, collagen, ligaments, and cardiac tissue); wound healing; works with vitamin C to promote healthy connective tissues
29
Role(s) of serine
precursor to glycine; metabolism of lipids and fatty acids; synthesis of pyrimidines, purines, creatine, and porphyrins
30
Role(s) of tyrosine
precursor to adrenal hormones (epinephrine, norepinephrine, and dopamine) and thyroid hormones (thyroxine); overall metabolism; function of adrenal glands, thyroid, and pituitary glands; mood elevator
31
Selenocysteine
21st amino acid; not coded for in genetic code; coded for in stop codon UGA
32
Pyrrolysine
22nd amino acid; coded for in stop codon UAG; not present in humans
33
Aminoacidopathies
class of inherited errors of metabolism in which there is an enzyme defect that inhibits the body's ability to metabolize certain amino acids
34
Phenylketonuria
PKU; autosomal recessive; 1 in 15,000 births; classic PKU- absence of phenylalanine hydroxylase (PAH) activity increases phenylalanine >1200 micromol/L, which causes brain damage; causes urine to have musty odor; mild PKU is partial deficiency of PAH activity with phenylalanine between 600-1200 micromol/L;
35
Normal phenylalanine in blood in infants
<120 micromol/liter; <2 mg/dL
36
Symptoms of PKU
retarded mental development; microcephaly
37
Hyperphenylalaninemia
phenylalanine elevation between 180-600 micromol/L without phenylketone elevation; deficiency in enzymes needed for regeneration and synthesis of BH4 (1-5% of all cases)
38
PKU treatment
early detection, diet with low levels of phenylalanine (infant and mom)
39
Tetrahydrobiopterin (BH4)
cofactor required for enzymatic hydroxylation of phenylalanine, tyrosine, and tryptophan; deficiency leads to elevation of phenylalanine and deficient production for neurotransmitters from tyrosine and tryptophan
40
PKU detection
Guthrie test, HPLC, HPLC-MS/MS, microfluorometric assay of dried blood filter disks; GC-MS;
41
Guthrie Test
semiquantitative, bacterial inhibition assay; sensitivity is 180 micromol/L (3mg/dL); blood is placed on agar dish that contains inhibitor of bacterial growth; if phenylalanine is present, inhibitor is overcome and bacteria grow
42
Microfluorometric assay
quantitative; based on complex formed with phenylalanine and ninhydrin which causes fluorescence
43
GC-MS
microwave assisted silylation; blood is rapidly derived with N,O, bis(trimethylsilyl)-trifluoroacetamine under microwave irradiation; analyzed by GCMS; confirmation method
44
Tyrosinemia
autosomal recessive; metabolic disorder of tyrosine catabolism; elevated tyrosine in blood and elevated succinylacetone (toxic metabolite formed when tyrosine cannot be metabolized) by MS/MS; low protein diet required
45
Alkaptornuria
autosomal recessive; 1 in 250,000 births; mutation in homogentisate oxidase (HGD) gene; required for metabolism of phenylalanine and tyrosine; elevated concentrations of homogentisic acid (HGA) in blood; symptoms present in 3rd decade of life; dark-blue/black pigmentation of of ears, nose, and tendons; small dark spots on sclera of eye; cause arthritis-like degeneration; urine mixed with air will result in brownish-black color due to oxidation of HGA; high dose Vitamin C
46
Maple Syrup Urine Disease
autosomal recessive; 1 in 185,000 births; absence or reduced activity of branched-chain alpha-ketoacid decarboxylase (BCKD); inhibits metabolism of leucine, isoleucine, and valine; maple syrup or burnt sugar smell of urine, breath, and skin; symptoms in infants include lethargy, vomiting, lack of appetite, and failure to thrive within 1 week of birth; dietary restriction of proteins; leucine concentration of >4mg/dL
47
Isovaleric Acidemia
1 in 250,000 births in US; mutation in isovaleryl-CoA dehydrogenase (IVD) gene; may be asymptomatic; distinctive odor of sweaty feet; may include failure to thrive, vomiting, lethargy; severe forms can result in permanent brain damage, nervous system damage, and death; protein restrictive diet and supplementation with glycine and carnitine
48
Homocystinuria
autosomal recessive, 1 in 200,00 births; mutations in CBS, MTHFR, MTR, MTRR, and MMADHC genes; most common is mutation in CBS gene; Guthrie test; symptoms include nearsightedness, dislocation of the lens in the eye, mental retardation, osteoporosis; methionine >2mg/dL
49
Citrullemia
urea cycle disorder; autosomal recessive
50
Argininosuccinic aciduria
autosomal recessive; urea cycle disorder; 1 in 70,000 births; lack enzyme argininosuccinic acid lyase (ASL); nitrogen accumulates in blood (ammonia); clinical symptoms start within a few days of life with lethargy and unwillingness to eat; high caloric protein restrictive diet, arginine supplement
51
Cystinuria
autosomal recessive; 1 in 10,000 births; mutation in SLC3A1 and SLC7A9 genes; elevated levels of cystine (also lysine, arginine, and ornithine); kidney stones, ureters, or bladder stones; other symptoms of hematuria, flank pain, urinary tract infections; increase of fluid uptake or penicillamine; diagnosed by cyanide nitroprusside which produces a red-purple color
52
Type II citrullinemia
mutation in SLC25A13 gene, which encodes for production of the protein citrin (transports molecules inside cell that are used in production and breakdown of simple sugars, etc); cells are prevented from making citrin, inhibits urea cycle; elevation of ammonia and other toxic substances; confusion, restlessness, memory loss, personality changes, seizures, and coma; high caloric, protein restrictive diet; arginine supplement
53
Methods of analysis-amino acids
blood drawn after 6-8 hours of fasting; collected in heparin tube and plasma removed immediately; hemolysis and contamination with white blood cells is unacceptable; deproteinization is performed within 30 min of sample collection and analysis performed immediately or sample stored below -20C; urine amino acids is performed on random specimen for screening and 24 hour urine for quantitative measurement
54
Methods of analysis-amino acids
blood drawn after 6-8 hours of fasting; collected in heparin tube and plasma removed immediately; hemolysis and contamination with white blood cells is unacceptable; deproteinization is performed within 30 min of sample collection and analysis performed immediately or sample stored below -20C; urine amino acids is performed on random specimen for screening and 24 hour urine for quantitative measurement-preserved with thymol; TLC is method of choice- can be 1 or 2 dimensional- stained with ninhydrin to visualize; ion-exchange chromatography with fluorescence detection; LC-MS/MS
55
normochromic normocytic anemia
type of anemia in which the circulating RBCs are the same size (normocytic) and have a normal red color (normochromic)

Clinical Chemistry Review (15 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions