Clinical Chemistry LAB CMBP

LIPID AND LIPOPROTEIN DETERMINATION

Question Answers
An unsaturated steroid alcohol with four rings and a single C-H
Cholesterol is synthesized from what?
What part of the cell gets the cholesterol synthesized?
What other forms does cholesterol have, where a hydroxyl group is linked with a fatty acid?
What is the classification of cholesteryl esters because of what charge?
Where are cholesteryl esters found?
What tube is used in cholesterol testing?
How many hours should a patient fast for cholesterol determination?
What is the temperature when sample for cholesterol is not on the gel separator tube?
What is the two principles of cholesterol determination?
What is the principles of chemical methods in cholesterol determination?
What are the two methods that causes color development?
What method causes a red color product?
What method produces a green color product?
What causes the red color product?
What causes the green color product?
What are all the general methods for cholesterol determination?
Enumerate the other methods involved in One-step Method
Enumerate the other methods involved in Two-step Method
Enumerate the other methods involved in Three-step Method
Enumerate the other methods involved in Four-step Method
What is the interference encountered in One-step Method
Enumerate the process involved in One-step Method
Enumerate the process involved in Two-step Method
Enumerate the process involved in Three-step Method
Enumerate the process involved in Four-step Method
What isolates cholesterol from protein?
What is collected from saponification of total sterols and esters?
What is the purpose of saponification in the Abell-Kendall method?
What do you call the non-enzymatic method in Cholesterol determination?
What do you call the enzymatic method in Cholesterol determination?
What do you use to hydrolyze cholesteryl esters in the Abell-Kendall method?
What do you use to extract unesterified cholesterol?
Abell-Kendall: Cholesterol + sulfuric acid +_____________ → Green Solution
What is the enzyme used in the first step of enzymatic method?
What is the enzyme used in the second step of enzymatic method?
What is the enzyme used in the third step of enzymatic method?
What is the product in the first step of enzymatic method?
What is the product in the first step of enzymatic method?
What is the product in the first step of enzymatic method?
Triglyceride is composed of three fatty acid molecules which is joined together by an ________?
What is the Step 1 in the non-enzymatic method in Triglyceride Measurement?
What is the Step 2 in the non-enzymatic method in Triglyceride Measurement?
What is the other name for non-enzymatic method?
What is the product in Step 2 of Triglyceride Measurement?
What is used to oxidize glycerol and form formaldehyde?
What is used to saponify triglycerides to produce glycerol and fatty acids?
 Clinical Chemistry LAB CMBP

What are the two methods under non-enzymatic methods in Triglyceride Measurement?
In the Van Handel and Zilversmith method, what is the chloroform-ethanol mixture used to
extract serum lipids?
In the Van Handel and Zilversmith method, what is used to remove phospholipids?
What is used to treat forlmaldehyde to form a blue-colored compound?
What is another name for the Hantzh Method?
What is used to treat forlmaldehyde to form a yellow-colored compound?
What method produces a blue-colored compound?
What method produces a yellow-colored compound?
What are the three steps of the enzymatic method in Triglyceride Determination?
What enzyme is used on step one of the enzymatic method in Triglyceride Determination?
What enzyme is used on step one of the enzymatic method in Triglyceride Determination?
How many hours should a patient fast for triglycerides measurement?
How many hours is the peak of plasma?
What causes the plasma to have higher level triglycerides than the serum?
What tubes can cause interferences in the triglycerides test?
What adsorbents removes interfering substances?
What is the composition of discoidal HDL?
What mechanism proposed to explain the anti-atherogenic property of HDL?
What is the density of the sample in the ultracentrifugation for lipoprotein measurement?
What is precipitated in Polyanion Precipitation for lipoprotein measurement?
Is centrifugation needed in polyanion precipitation?
What reagents are used in the quantification of HDL?
Where is the HDL found in the centrifugated serum? What kind of apolipoprotein are these?
It is mixed with the supernatant to quantitate HDL concentrations.
What is the decreasing order of the density of lipoproteins?
What is the pH level on the mobility at cellulose acetate or agarose?
What is the order of mobility going to the anode of the lipoproteins?
What is at the origin of electrophoresis of lipoproteins?
What are the names of the lipoproteins in electrophoresis?
The separation of lipoproteins are based on what?
What is the equation for LDL called?
What is the formula for the LDL?

NON-PROTEIN NITROGENOUS COMPOUNDS DETERMINATION

Question Answers
What has the highest concentration of NPN found in the blood? Urea
What is the primary product of protein metabolism that is excreted? Urea
Where is urea synthesized? Liver
What is the name of the cycle where urea is synthesized from amino groups and free ammonia? Urea cycle
How is the amount of urea in the blood determined? Protein Diet, Rate of
Protein Catabolism, and
Function of the kidneys
What are the two types of enzymatic methods in Nitrogen Determination? Indirect and Direct
Method
What are the methods under Indirect Method in Nitrogen Determination? GLDH coupled
enzymatic reaction,
Indicator Dye,
Conductimetric, and
Isotope Dilution Mass
Spectrometry
 Clinical Chemistry LAB CMBP

What is the method under Direct Method in Nitrogen Determination? Fearson’s Reaction
What is the general principle of the enzymatic method under Nitrogen Determination? NH3 Formation
What reaction forms a yellow color in the indicator dye? Nessler’s reaction
What reaction forma a blue color in the indicator dye? Berthelot reaction
What is the method that measures the rate at which conductivity increases as NH4 id produced Conductimeteric
from urea?
What is used to measure the rate at which conductivity increases as NH4 id produced from urea? Ammonia-selective
electrode
What method detects and quantifies characteristic fragments following ionization using Isotope Dilution Mass
isotopically labeled compounds? Spectrometry
What is formed from the reaction of urea with diacetyl monoxime? Yellow solution (Diazine
derivative)
What is added to enhance color formation and eliminate protein interference? Arsenic
thiosemicarbazide
What reaction is called when yellow solution is formed when adding diacetyl monoxime? Fearson’s reaction
What anticoagulants must be avoided in Nitrogen Determination? Ammonium and fluoride
salts
What is the byproduct of purine nucleic acid catabolism? Uric Acid
When there is high concentrations of uric acid deposited at joints, it can cause? Uric Acid
What are the methods in Uric Acid Determination? Enzymatic, Chemical,
and Isotope Dilution,
Mass Spectrometry
What is the method under Chemical Method in Uric Acid Determination? PTA (Caraway method)
The method mentioned above (PTA) forms what color solution? Blue
What reagent is used to oxidize uric acid to allantoin and CO2 in an alkaline solution? Phosphotungstic acid
reagent
What enzyme is used to oxidize uric acid to form allantoin, carbon dioxide, and hydrogen Uricase
peroxide?
What is the wavelength used in differential absorption of uric acid? 293 nm
What are the three methods in the enzymatic method of Uric Acid Determination? Enzymatic H2O2
Production, Enzymativ
UV, Scpectrophotometric
(Blauch and Koch)
What are the two coupled enzymes in H2O2 production? Catalase and Peroxidase
What method needs special instrumentation and optical cells Enzymatic: UV
What is the other term for the spectrophotometric method in enzymatic method? Blauch and Koch
What is the proposed reference method in Uric Acid Determination? Isotope Dilution Mass
Spectrometry
What results would affect Uric Acid Determination Hemoglobin and
bilirubin (greater than 20
mg/dL0
How many days the uric acid sample stable in room temperature? 2-3 days
How many days the uric acid sample stable in refrigerator temperature? 3-7 days
What is synthesized in muscles and excreted to the plasma at a rate proportional to muscle mass? Creatinine
Where is the answer above created from? Creatine and Creatine
Phosphate
What are the three amino acids where creatinine is primarily synthesized from? Arganine, glycine, and
methionine
What combines to form the cyclic compound creatine that diffuses into the plasma and is excreted Phosphoric acid and
in the urine? water
What are the three methods under Creatinine Determination? Chemical, Enzymatic,
Isotope Mass Dilution,
Spectrometry
What is simple and nonspecific in the chemical method of Creatinine Determination? Colorimetric: End Point
What is rapid increase of specificity in the chemical method of Creatinine Determination? Colorimetric: Kinetic
What are the four methods under chemical method of Creatinine Determination? Direct jaffe, Kinetic
 Clinical Chemistry LAB CMBP

Jaffe, Jaffe with

adsorbent, Jaffe without
adsorbent
It is the formation of a red tautomer of creatinine picrate when creatinine in serum is made to Direct jaffe
react with a freshly prepared alkaline sodium picrate solution.
What is added to creatinine in Direct jaffe? Alkaline picrate
What is the product in Direct Jaffe? Red orange solution
It is the rate of change of absorbance (color formation) is detected to avoid interference of non- Jaffe-kinetic
creatinine chromogens.
What causes negative bias in Jaffe-kinetic method? Bilirubin and
hemoglobin
What causes positive bias in Jaffe-kinetic method? a-ketoacids and
cephalosporin
What reagent is used to adsorb creatinine? Fuller’s earth (aluminum
magnesium silicate) and
Lloyd’s reagent (sodium
aluminum silicate)
What is used to elute creatinine? Alkaline Picrate
What does adsorbent improve? Specificity
What method uses protein-free filtrate with creatinine and alkaline picrate? Jaffe without adsorbent
What are the methods under enzymatic method of Creatinine Determination? Dry Slide Analyzer,
Creatininase-CK,
Creatininase- H2O2,
Creatinase Method
What are used under the Dry Slide Analyzer? Creatininase (creatinine
aminohydrolase),
Creatine (creatinine
aminohydrolase),
Sarcosine oxidase,
Peroxidase
What is formed when creatinine is hydrolyzed by creatinase? N-methylation and
ammonia
What is formed on the reaction of ammonia and alpha ketoglutarate Glutamate and NAD
It is the detection of characteristic fragments following ionization Isotopic Dilution Mass
Spectrometry
What is the highly specific and accepted reference method for Creatinine Determination? Isotopic Dilution Mass
Spectrometry
What inhibits enzymatic reactions that utilize peroxidase as a reagent? Ascorbate
What is the cause of a negative bias in both Jaffe and enzymatic methods? Bilirubin

RENAL FUNCTION
Question Answers
What are the waste products in the renal function? Urea and Creatinine
What is the rate at which creatinine and urea are removed or cleared from the blood into the urine Clearance
How is clearance expressed? Mililiters per minute
What is the standard laboratory method for for determining GFR (glomerular filtration rate)? Creatinine Clearance
What is the first clearance test performed? Urea Clearance
What is administered in the old test to determine the GFR? Inulin
What is used to evaluate potential living kidney transplant donors? Iohalamate
What is the ideal substance for the measurement of clearance? Creatinine
What is the formula or creatinine clearance? ------------
It is an endogenous metabolic product synthesized at a constant rate? Creatinine
How is creatinine cleared? Glomerular Filtration
Where is creatinine slightly secreted? Proximal Tubule
 Clinical Chemistry LAB CMBP

What is included in specimen collection of creatinine clearance? 24 hour urine specimen

and serum creatinine
value
What is calculated when serum creatinine level is reported? Estimated Glomerular
Filtration Rate
GFR can be for the early detection of? Chronic Kidney Disease
(CKD)
What are the 3 formulae used for Estimated GFR? Cockcroft- Gault
Formula, Modification of
Diet in Renal Disease
Formula, and CKD-EPI
Formula
What formula is not corrected for body surface? Cockgroft-Gault Formula
What formula includes age, race, gender, and serum creatinine? Modification of Diet in
Renal Diseases Formula
What formula includes age, race, gender, and serum creatinine but performs with less bias? Chronic Kidney Disease
Epidemiology
Collaboration (CKD-
EPI) Formula
It is a low molecular weight protein that is produced at a steady rate in body tissues? Cystatin C
What does a rise in Cystatin C do in the amounts of creatinine and GFR? Increase in creatinine and
decrease in GFR
What is the random fluctuation around a homeostatic setting point? Biological variation
What is the fluctuation of a homeostatic setting for a single individual? Within-subject
Biological Variation
What is the fluctuation of a homeostatic setting for multiple individuals? Between-Subject
Biological Variation
What is the correlation of creatinine in biological variation? Lower in within subject
Higher in between
Variation
What is the correlation of cystatin C? It is higher that creatinine
in both variations
What is the small, non glycosylated peptide found on the surface of nucleated cells? B2- Microglobulin
What is the low-molecular weight protein associated with skeletal and cardiac injury? Myoglobin
What is used to bind and transport oxygen in muscle cells? Myoglobin
What describes the presence of albumin in the urine? Albuminuria
What is the albumin to creatinine ratio? Greater than 30mg/g
What is the 25kDs protein expressed by neutrophils and epithelial cells including the proximal Neutrophil gelatinase-
tubule? associated lipocalin
(NGAL)
What is the first FDA-cleared test in determining risk for AKI in 12 hours? NephroCheck
What are the two biomarkers used in NephroCheck? TIMP-2 and IGFBP-7
What is used as an indicator for glucose status and hepatic-biliary function? Urinalysis
How should the urine specimen be obtained or collected? Clean midtream catch or
catheterization
The specimen should be analyzed within how many hours of collection? 1 hour
What is the temperature when specimen is not analyzed for 1 hour? 2-8 degrees Celsius for
not more than 8 hours
The is the more concentrated color of urine? Darker color
What is the reason for yellow and amber urine? Urochromes
What causes yellowish-brown to green color? Bile pigment oxidation
What causes red and green urine color? Porphyrins
What causes reddish brown color? Hemoglobin and RBC
What causes the brownish black color? Alkaptonuria and
malignant melanoma
What causes the pungent odor of fresh urine? Volatile aromatic acids
 Clinical Chemistry LAB CMBP

What causes the fecal smell in urine? UTI

What causes the fruity smell of the urine in diabetics? Ketones
Where is turbidity seen? Gross bacteriruria
Where is cloudy appearance seen? Hematuria
Where is thread-like cloudiness seen? Full of mucus
What is responsible in the rabidity of alkaline urine? Amorphous phosphates
and carbonates
What is responsible in the rabidity of acidic urine? Amorphous urates
What gives an indication of the density of fluid? Specific Gravity
What is used to assess the state of hydration or dehydration? Specific Gravity
What is used as an indicator of the concentrating ability of kidneys? Specific Gravity
How is specific gravity measured? Refractive index
What is the normal range for the SG in urine? 1.003- 1.035 g/mL
What is used in routine chemical analysis of urine? Reagent strips or
dipsticks
What method does automate chemical analysis instruments of urine use? Reflectance Photometry
What is most commonly seen in Glucosuria? Glucose
What is the hallmark presence of diabetes mellitus and ketonuria? Ketones
What is seen in proteinuria? Proteins
What is detected when there are gram negative bacteria? Nitrite
What does a positive dipstick for esterase mean? Presence of WBC
What is the result of hemoglobin degradation? Bilirubin
What is found in trace amounts in urine? Urobilinogen
What is found when there are lysed RBC in urine? Blood
What causes the sparkling effect in granules of WBC? Hypotonic Urine
What do you call the sparkling granules of WBC? Glitter cells
What are considered abnormal amount of RBC? Greater than 2
What are considered abnormal amount of WBC? Greater than 5
What are the three epithelial cells seen in urine? vaginal, renal, and
bladder epithelial cells
What kind of cells is most the size of the RBC and are extremely refractile? Yeast Cells
What parasite is commonly infected in children? Entorobius vernicularis
(pinworm)
What parasite is intensely motile and sexually transmitted? Trichomonas vaginalis
What is the true urinary parasite? Schistosoma
haematobium
How many bacteria is clinically significant? 20 organisms in HPF
What are the gram-negative coliform pathogens seen in urine? Escherichia coli and
Proteus spp.
What do you call the precipitated, cylindrical impressions of the nephrons? Casts
What does cast comprise of? Uromucoid (Tamm-
Horsfall mucoprotein)
How are casts classified when patient has several renal diseases? Cytospin centrifuge and
Papanicolaou staining
What are the only one where low power is used? Casts
Where are casts often located in the PBS? Edges of cover slip
Its presence indicates glomerular leakage of protein. Hyaline
The matrix are clear and gelatinous with particulate matter. Hyaline
Where are large numbers of granular casts found? Chronic lead toxicity and
pyelonephritis
What is used for the diagnostic for glomerular inflammation? RBC casts
What is used for the diagnostic for nephrons? WBC casts
 Clinical Chemistry LAB CMBP

What is formed by fusion of renal tubular epithelia after desquamation? Epithelial casts
What are uniformly yellow, refractile, and brittle appearing with sharply defined broken edges? Waxy casts
What are abnormal, coarse, granular cats with lipid inclusions that appear as refractile globules of Fatty casts
different sizes?
What is two to six times wider than “regular” casts? Broad casts
What indicates tubular inflammation and discoloration? Waxy casts
What are the acidic crystals in urine? Cystine Crystals,
Cholesterol crystals, Uric
acid crystals,
Amorphous urates,
Calcium Oxalate
What are the alkaline crystals in urine? Amorphous phosphates,
Calcium carbonate,
Calcium carbonate
crystals, Triple phosphate
crystals, Ammonium
biurate crystals
What are normal colorless octahedrons or “envelopes” with starlike appearance? Calcium Oxalate
What are normal pink-red masses that look like grains of sand? Amorphous urates
What are yellow to brown crystals that appear in extremely irregular shapes? Uric acid crystals
What are the irregular shapes of uric acid crystals? Rosettes, prisms,
rhomboids
What are clear flat rectangular planes with notched corners? Cholesterol crystals
What is colorless, refreactile, nearly flat hexagons? Cystine Crystals
Where are cystine crystals observed? Homocystinuria and
cystinuria
What are normal crystals that appear colorless and fine resembling sand? Amorphous phosphates
What are small, colorless, dumbells or sphere crystals? Calcium carbonate
crystals
What are crystals that have colorless prisims of 3-6 sides resembling coffins? Triple phosphate crystals
What are crystals that appear as spiny, yellow-brown spheres or thorn apples? Ammonium biurate
crystals
What are the pathological crystals? Sulfonamide, leucine,
and tyrosine crystals
What are abnormal precipitates shaped like yellow-brown sheaves, clusters, or needles? Sulfonamide crystal
What crystals appear yellowish brown in color with concentric circles having radial striations Leucine crystal
resembling dark rings of a tree trunk?
What crystal are shaped like clusters of smooth yellow needles or spheres? Tyrosine crystals

AMINO ACIDS
Question Answers
What are simple organic compounds that serve as building blocks of proteins? Amino acids
What does a single amino acid contain? v
What is the N-terminal end of the amino group? -NH2
What is the C-terminal end of the carboxyl group? -COOH
Where is the N-terminal end and C-terminal end bonded to form an amino acid? a-carbon
Amino acids are ______, meaning they have acidic and basic tendencies. Amphoteric
What can an amino acid accept? Proton (basic) forming
-NH3+
What can an amino acid donate? Proton (acidic) forming
-COO-
What are amino acids classified as since their net charge is neutral? Zwitterions
How to amino acids differ from one another? Composition of the R
group called side chains
 Clinical Chemistry LAB CMBP

What group is used to link the two amino acids? Carboxyl group
What do you call amino acids connected with peptide bonds? Polypeptide bonds
How are the content and arrangement of amino acids determined? Sequence of nucleotide
bases
What does gastrin in the stomach stimulate? Secretion of HCL and
proteolytic enzymes
(pepsin)
What is used to neutralize the HCl in the small intestines? What organ secreted it? Sodium bicarbonate by
the pancreas
What does the pancreas secrete to protect the intestinal lining? Secretin
What is secreted by the small intestines that stimulates the release of proteolytic enzymes? Secretin and
cholecystokinin
What are examples of proteolytic enzymes? Trypsin and
chymotrypsin from the
pancreas and bile from
the gallbladder
Where are amino acids absorbed? Intestinal lumen through
cotransporters
What results when peptidase cleaves peptide bonds? Free amino acids
What transports anion acids from the small intestines to the bloodstream then to the liver via the Facilitative transporters
hepatic portal?
Where will amino acids synthesize into proteins and nonproteins nitrogenous compounds? Liver
Where does pepsin break down proteins into peptides? Stomach
Where does peptides break down into amino acids? Small intestines
What does stomach cells secrete? Pepsin and HCL
What does small intestines secrete? Secretin and
Cholecystokinin
What does acinar cells secrete? Trypsin, Chymotrypsin,
Elastase, Sodium
bicarbonate
What are essential amino acids? It must be acquired
through dietary intake.
What are the nine essential amino acids? Histidine, isoleucine,
leucine, lysine,
methionine,
phenylalanine, threonine,
tryptophan, valine
What amino acid helps to grow and repair body tissues Histidine
What amino acid maintains myelin sheaths Histidine
What amino acid synthesizes red and white blood cells? Histidine
What protects the body from toxicity of heavy metals? Histidine
What serves as a source or carbon atoms in DNA/RNA synthesis? Histidine
What are the branched-chain amino acid group composition? Isoleucine, leucine, and
valine
What is essential for wound healing, immunity, glucose homeostasis, and hemoglobin formation? Isoleucine
What is essential for the regulation of blood glucose, wound healing, and prevention of protein Leucine
degradation?
What aids in the tertiary structure of proteins and promoted mental health and muscle Valine
coordination?
What amino acid plays a role in the production of antibodies? Lysine
What amino acid is required for maintaining healthy tissues? Lysine
What amino acids helps in conservation of calcium? Lysine
What amino acid has a role in the formation of collagen? Lysine
What amino acid helps to initiate translation of mRNA and stabilize protein structure? Methionine
What amino acid is a source of sulfur? Methionine
What amino acid is an important cellular antioxidant? Methionine
 Clinical Chemistry LAB CMBP

What amino acid assists in the breakdown of fats? Methionine

What amino acids helps to diminish muscle weakness? Methionine
What amino acid prevents brittle hair? Methionine
What reacts with ATP in the synthesis of substances? Methionine
What is the metabolic precursor for tyrosine? Phenylalanine
What is the precursor for catecholamines which maintains homeostasis? Phenylalanine
What amino acid is important in the formation od collagen, elastin, and tooth enamel? Threonine
What amino acid is important in the production f neurotransmitters and in the overall health of the Threonine
nervous system?
What amino acid maintains proper body balance? Threonine
What amino acid is a metabolic precursor for serotonin and melatonin? Tryptophan
What amino acid is a natural relaxant that helps alleviate insomnia? Tryptophan
What amino acid is essential to produce niacin? Tryptophan
What are the nonessential amino acids in our body? Alanine, asparagine,
aspartic acid, glutamic
acid, selenocysteine, and
serine
What amino acid is the product of the breakdown of DNA, anserine, and carnosine? Alanine
What amino acid is formed because of glycolysis and the conversion of pyruvate to a- Alanine
ketoglutarate?
What amino acid plays a role in the transfer of nitrogen from tissues to the liver ? Alanine
What amino acid is a ketogenic amine? Alanine
What amino acid serves a source of energy for the CNS, brain, and muscle tissues? Alanine
What amino acid helps in reducing the buildup of toxic substances when muscle protein is broken Alanine
down?
What amino acid is derived from aspartic acid and ATP through transamidation? Asparagine
What is the process where asparagine is derived from aspartic acid and ATP? Transamidation
What is the process where an amide group is transferred from one compound to another? Transamidation
What is the process by which asn amine group is introduced into an organic molecule? Amination
What is the process where there is a transfer of an amino acid to an a-ketoacid? Transamination
What amino acid is synthesized from oxaloacetate through transamination in the citric acid cycle Aspartic acid or aspartate
and the urea cycle?
What amino acid is the precursor for other amino acids (asparagine, lysine, methionine, threonine, Aspartic acid or aspartate
and isoleucine)
What amino acid serves as a neurotransmitter and participates in the generation of glucose from Aspartic acid or aspartate
non-carbohydrate substances?
What do you call the process where there is a generation of glucose from non-carbohydrate Glucogenesis
substances?
Amino acid that is produced from the transamination of amino acids such as alanine and aspartic Glutamic acid or
acid glutamate
Amino acid that serves as a neurotransmitter and has an important role in metabolism of fats and Glutamic acid or
carbohydrates glutamate
Amino acid that is not coded directly in the genetic code Selenocysteine
Codon that is encoded in selenocysteine UGA codon (stop codon)
Amino acid that has a specialized tRNA Selenocysteine
What does the name selenocysteine mean? Selenium analogue of
cysteine (selenium atom
replaces sulfur)
What amino acid is present in formate dehydrogenase, glycine reductase, and some hydrogenase? Selenocysteine
What amino acid is synthesized from 3-phosphoglycerate (intermediate in glycolysis) Serine
Amino acid needed for proper metabolism of lipids and fatty acids Serine
What are the semi-essential or conditionally essential amino acids? Arginine, cysteine,
glutamine, glycine,
proline, and tyrosine
 Clinical Chemistry LAB CMBP

What will happen if a conditionally essential amino acid is produced from an essential amino Deficiency in the
acid? essential amino acid
Amino acid found at the catalytic site in proteins and enzymes due to its amine-containing side Arginine
chain
Amino acid that has the role in the conversion of ammonia into urea Arginine
Amino acid that is potentially toxic where it is reabsorbed during digestion as cystine Cysteine
Cysteine can also be synthesized in vivo from what? Methionine
Amino acid found in beta-keratin Cysteine
Amino acid that is important in collagen formation Cysteine
Amino acid synthesized from glutamic acid and an addition of an ammonia group Glutamine
Amino acid that can donate the ammonia group to form urea Glutamine
Amino acid for the regulation of ammonia (which is a toxic substance) Glutamine
Amino acid synthesized from the amino acid serine Glycine
Amino acid that limits muscle degeneration Glycine
Amino acid that is used by the liver in the detoxification of compounds Glycine
Amino acid produced from glutamic acid and other amino acids Proline
Amino acid that serves ad the precursor of hydroxyproline Proline
What are manufactured into collagen, tendons, ligaments, and cardiac tissues Hydroxyproline
Amino acid responsible for strengthening pf cartilage and joints Proline
Amino acid synthesized from phenylalanine Tyrosine
Amino acid that serves ad a precursor for adrenal and thyroid hormones Tyrosine
Amino acid that stimulates metabolism and the nervous system Tyrosine
Amino acid that acts as an mood elevator Tyrosine
Class of inborn errors of metabolism in which an enzyme defect inhibits the body’s ability to Aminoacidopathies
metabolize certain amino acids
Early diagnosis of numerous inborn errors of metabolism Newborn screening
Samples used for aminoacidopathoies Urine sample
Sample that is analyzed to aid in diagnosis of neurotransmitter disorders Cerebrospinal fluid
Hours of fasting to avoid the effect of absorbed amino acids originating from dietary proteins 6-8 hours
Anticoagulant used for aminoacidopathoies Heparin
Number of hours before the removal of plasma from the tube 2 hours
Delayed samples should be Refrigerated for 24 hours
Frozen for 1 month
Method used to quantitate amino acids and their metabolites HPLC-MS/MS
Method for detection od inborn error of metabolism Genetic assays
Method to have higher specificity and greater sensitivity MS/MS