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analytes elevated in women
iron, a-lipoprotein, cholesterol, y-globulin
analytes elevated during AM
cortisol, aldosterone, iron, ACTH
analytes elevated during PM
TH, GH, ACP, TSH
analytes elevated in black people
CK, LD, IgG, IgA, TP
analytes elevated during hemoconcentration
calcium, iron, sodium, enzymes, hematocrit, proteins
analytes that need to be placed in an ice slurry
lactic acid, ammonia, blood gases
analytes decreased after recent food intake
chlorides, amylase, phosphorous, potassium, ALP
analytes decreased in exercise
cholesterol, triglycerides
analytes decreased in black people
albumin
analytes decreased when specimen is not examined within 30 minutes
pH and pCO2
blood specimen normally used in chemistry tests
serum
blood specimen normally used in hematology
whole blood
blood specimen containing fibrinogen
plasma
blood specimen whose composition is affected by metabolic activity of the tissue
venous blood
blood specimen that has a uniform composition throughout the body
arterial blood
blood specimen whose composition is a mixture of venous and arterial blood with the addition of tissue fluid
capillary blood
percent of blood that is fluid
55%
capillary blood is mostly composed of
arterial blood
analyte affected when pH of serum reach 8.5
ACP (decreases)
analyte affected when there are changes in the red cell
increased serum potassium, phosphorous, magnesium permeability
analyte affected when a frozen specimen is thawed
increased alkaline phosphatase
when is the tourniquet released during ETS
before the last tube is filled
what information is required in the label for venipuncture
patient's name, date of birth, date and time of collection, phlebotomist's initials
color of gauge 21 needle
green
color of gauge 22 needle
black
color of gauge 23 needle
blue
inert clays are examples of what type of tube additive
clot activators
examples of inert clays
diatomite(celite)
what initiates clotting in your SST tube
silica pearls
what color is your SST tube
gold
tube for STAT serum testing
orange tube
tube that converts fibrinogen to fibrin
orange tube
additive in your green tube
heparin
mechanism of action of heparin
inhibits thrombin and factors Xa
heparinized blood is used for
blood pH, blood gases, electrolytes, calcium
how many times is your green tube inverted
8x
analytes increased in your lavender tube
sodium, potassium, PT, PTT
analytes decreased in your lavender tube
calcium, iron
when are your black tubes collected
after EDTA tubes
what is the additive in your lavender tube
dipotassium EDTA
what is collected after your gray tube
ACD, royal blue tube
what is the purpose of your royal blue tube
trace elements
angle of puncture for arterial collection in your brachial artery
45-60 degrees
angle of puncture for arterial collection in your femoral artery
90 degrees
local immediate complications in ETS
hemoconcentration, failure of blood to enter syringe, syncope, circulatory failure
local delayed complications in ETS
hematoma, thrombosis, thrombophlebitis
general delayed complications in ETS
HIV, hepatitis B
skin puncture site ideal for the detection of histiocytes
free edges of earlobes
analytes increased in your lipemic samples
calcium, albumin, inorganic phosphates
analytes decreased in your lipemic samples
creatine kinase, urease, bilirubin, total protein, amylase
anticoagulants that causes dilution errors
oxalates
anticoagulants that inhibit plasma enzyme activities
EDTA, fluoride
anticoagulants that inhibit amylase
oxalates, citrates
anticoagulants that inhibit LD, ACP
oxalates
anticoagulants that elevate calcium
oxalates, citrates, EDTA
why should blood never be drawn in a site where IV medication is running
false low
analytes elevated when using betadine/povidone iodine
phosphorous, uric acid, potassium
general formula of amino acids
RCH(NH2)COOH
the amino group of amino acids is composed of
one nitrogen and two hydrogen (NH2)
the carboxyl group of amino acids is composed of
one carbon and two oxygen (COO-)
the carboxyl and amino group of amino acids is linked together by
alpha carbon and alpha hydrogen (CH)
essential amino acids
phenylalanine, valine, threonine, methionine, tryptophan, histidine, isoleucine, leucine, lysine (PVT MT HILL)
none essential amino acids
glutamic acid, aspartic acid, glutamine, asparagine, glycine, alanine, proline, cysteine, tyrosine, serine
these two processes occur at physiologic(neutral) pH near 7.4
protonation and deprotonation
addition of hydrogen (H+) to your amino group
protonation
removal of hydrogen (H+) to your carboxyl group
deprotonation
at low pH your amino acid has __________ charge
positive charge
at high pH your amino acid has _________ charge
negative charge
pH at which your amino acid will have no hydrogen ions
high pH
pH at which your amino acid will mostly have hydrogen ions
low pH
this is an index of water solubility of the side chain of an amino acid
hydropathy index
as the hydropathy index increases, the amino acid's insolubility...
increases
the amino acid that is most insoluble in water
isoleucine
amino acid groups which have high water solubility and low hydropathy
amide and hydroxyl groups
amino acid groups which have low water solubility and high hydropathy
amino acids with allopathic or aromatic side chains
acidic amino acids
glutamic acid, aspartic acid
basic amino acids
lysine, arginine, histidine
semi-essential amino acid
arginine
the body's primary source of amino acids for protein synthesis
dietary protein
another source of free amino acids; aka recycled amino acids
endogenous protein turnover
adult daily protein requirement
0.8g/kg of body weight
situations in which increased protein demand is observed
growth, pregnancy, lactation, stasis or protein loss, disease states with increased protein breakdown
a diet with adequate calories with low protein intake
kwashiorkor syndrome
a diet with inadequate calories and protein
marasmus
serum albumin values in kwashiorkor syndrome
decreased
traits observed in kwashiorkor syndrome
edema, ascites, growth failure, immune deficiency, apathy
moon face is observed in
kwashiorkor syndrome
composed of polymers of amino acids that are linked together and form into chains
protein
an amide linkage that is formed when an alpha amino group of one amino acid is bound together covalently to another amino acid's carboxyl group
peptide bond
two or more amino acids linked by peptide bonds
peptide
protein synthesis occurs from __-terminal to __-terminal
N->C
naming of the peptide is based on what type of amino acid is formed in the __-terminal residue
N
where are plasma proteins synthesized
hepatocytes of the liver
what synthesizes immunoglobulins
plasma cells/B cells (lymphocytes) in the bone marrow
purines
adenine and guanine
pyrimidines
cytosine, thymine, uracil
where does transcription occur
nucleus
where does translation occur
cytoplasm
adenine pairs with
uracil/thymine
guanine pairs with
cytosine