Study your flashcards anywhere!

Download the official Cram app for free >

  • Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off

How to study your flashcards.

Right/Left arrow keys: Navigate between flashcards.right arrow keyleft arrow key

Up/Down arrow keys: Flip the card between the front and back.down keyup key

H key: Show hint (3rd side).h key

A key: Read text to speech.a key


Play button


Play button




Click to flip

212 Cards in this Set

  • Front
  • Back
whats unique about proteins vs carbs
carbs do not contain nitrogen or sulfur
what does the alpha carbon mean
the alpha carbon means there are different functional groups attached to each carbon
the carboxy group gives acidic or basic qualities
the carboxy gives acidic qualities, it is a proton donating group
the amine gives acidic or basic qualities
the amine gives basic qualities, it is a proton accepting group
any protein that has a metal ion would be a
any protein with a carb attached woiuld be a
any protein with a carb attached woiuld be a glycoprotein
amino acids are called amphoteric because
they can have either a positive or negative charge
do carbohydrates ever have a charge
as soon as you put a carbohydrate in an acid environment (h30) you will get a protein with a more acidic nature, meaning that proton will find a home with the _______, leaving a _____ charged _______
in an acid environment (h30) you will get a protein with more acidic nature, meaning that proton will find a home with the carboxy group, leaving a positively charged amino group
the charge of the protein can be changed by changing the ___ of the solution the protein is in
we operate at a pH of
if you put a protien in an alkaline soln it will have a ___ charge
if you put a protein in an alkaline solution it will have a negative charge
if you put the protein in a acidic enviornemnt it will have a _____ charge
if you put the protein in an acidic environment it will have a positive charge
what is the charge of leucine
what is the polarity of leucine
what is the charge of arginine
what is the polaritiy of arginine
what is the charge of aspartic acid
what is the polarity of aspartic acid
what is the polarity of serine
what is the charge of serine
what non polar amino acid did we talk about
what two none charged amino acids did we talk about
leucine and serine
how many naturally occuring amino acids are there
what makes each amino acid unique
the r group
leucine contains amino acids that are not charged and not polar so it does not like
amino acids that are polar are more on the ___ of the protein vs the non polar ones who like to be on the ___,
you will find amino acids that are polar more on the outside of the protein vs the non polar ones whou would like to be on the inside furthest away from the water
arginine has a net positive charge at physiological pH and that makes it ___ meaning it likes to be around water
you have a group of amino acids that have a unique group like an extra hydroxy which like to be near water, which causes it to be ___ even though it does not have a net charge
so a non polar will atract a
non polar
amino acids are going to react with eachother through there ___ to form a peptide bond
individual amino acids are going to react with each other through their amine group and hydroxide to form a peptide bond
protein synthetases are basically enzymes that __ water from amino acids, allowing for covalent peptide linkages
remove water
peptide bonds provide the __ structure which links the amino acids to one and another
primary structure
secondary structure is
these peptide linkages attract to help fold the protein
secondary and tertiary type of reactions are those that involve things like
van der waals interactions and hydrogen bonds, and ionic interaction, as well as disulfide linkages
secondary and tertiary structure is how proteins are
arranged in 3d
quaternary structure is
interactions between subunits in the protein, whereas myoglobin exists as a single protein, hemoglobin is made of four globin chains
does any protein digestion occur in the mouth?
where does protein digestion start
in the stomach
what is the pH of the stomach
pepsin is
nonspecific and prefers hydrophobic amino acids. it looks at polars connected to polars connected to positive connected to negative to non polar to non polar
pepsin will cleave after a ____ bond
non polar bond
in the small intestine enzymes coming from the ____, endopeptidases, will go to the inside of the protein and cleave
will go to the inside of the protein and start cleaving, by putting back in water
endopeptidases in the small intestine are
trypsin and chymotrypsin
the special enzyme to digest elastin, the protein in the skin is called
exopeptidases go towards the end and cleave with
either with an a aminopeptidase or a carboxypeptidase
where does protein absorption take place
in the microvilli via active transport of each amino acid, polar, charged, non polar, non charged
proteion absoprtion and idgestion occurs via the
microvilli of the digestive tract
what three systems are in the microvilli
the circulatory system, the lymphatic system, and the connective tissue
amino acids are going to be absorbed via the ____ system within the villus
where are the enzymes that break down carbs
in the brush border of the villi
1/3 of your body protein is made from
fibrous proteins, like colagen
elastins are going to be found in
arteries and tendons
what proteins make up hair
myosins are in
fibrin in sformed from
albumins are ___ in pure water and ___ salt concentrations
albumins are soluble in pure water and low salt concentrations
globulins are ___ in pure whater but ____ in salt concentrations less than ___%
globulins are insoluble in pure water but soluble in salt solutions less than 20%
our body has a slaine level that is
0.85 percent
when you talk about total protein you are talking about
all the protein in the blood
the units for albumin is
how many proteins have been identified in plasma?
hyperproteinemia is a
a increase in protein concentrations, relatively as seen in dehydration, or absolutely as seen in multiple myeloma and acute phase reactions
multiple myeloma is a cancer in the
bone marrow
cancerous plasma cells are making increased concentrations of either whole or fragment antibodies in
multiple myeloma
when you are experieincing any kind of stress, there is goin tto be a fight or flight response with or without epinephrin
acute phase reaction
is an absolute decrease or relative decrease in total protein
is a major causing of having an absolute decrease in protein, where albumin is bein glost in gram quantities
nephrotic syndrome
will lead to a absolute decrease in protein because the liver is the major synthesizer of proteins found in plasma except for the immunoglobulins
liver dysfunction
burns will cause a ____ in patients total protein
absolute decrease
starvation will cause a ____ in patients total protein
absolute decrease
where are antibodies made
in the bone marrow or certain parts of the spleen
is in underdeveloped 3rd world countries with lots of stasrvation, what happens is when child 1 gets born and is being fed breast milk, child 1 is thriving, then child 2 is born and child number 1 is deposed so baby 2 can eat
kwashiorkor syndrome
patients who have salt retention, will also mean water retention meaning you will have a _____ in total protein
relative decrease
what is the reference method for glucose determination
hexokinase method
what is the reference method for protein
kjeldal method
it is a kind of blunt force method that measures total protien by nnitrogen, it is not a method used clinically because the heat required to do it, but all other methods developed are going to be comparted to this method
kjeldahl method
is to protein as glucose oxygenase or dehydrogenase is to glucose
the buiret
what is the reagent in the buiret method
copper in the plus 2 state
protein with at least 2 peptide bonds at an alkaline pH will react with copper to form a
colored chelate
the copper and protein complex in the biuret method will have a ++++ color
is the buiret method directly proportional
yes it is
does the biuret method follow beers law
what are the requirments for the buiret sample
may not be hemolyzed, may not be lipemic, and plasma could be used but usually its serum
whats the difference between plasma and serum
serum does not contain fibrinogen
how long can the total protein sample be stored and at wha ttemperature
for a week at rt
what is the reference range for fibrinogen
when you go from laying down to standing up, what is the change in your plasma water volume
if a tourniquet is left to long on the arm, what can that do to total protein
what will bilirubin do to total protein
increase it
what three methods can we use to quantify total protein
refractive index, ultraviolet absorption at 280nm, and micromethods
the refractive indexi of water is on the total solid scale
proteins in general absorp at a wavelength of
ultraviolet 280
is a colorimetric, directly proportional method of quantifiying total protein
bicinchonic acid method (BCA)
a colorimetric method using a very stable dye, that is directly proprtional to quantified protein
coomassie blue
is a nepholometric method for quantifying total protein
5% sulfosalicylic acid
there is going to be one PH environment that you can put this protein into where the number of negative charges equals the positive charges this is called the
isoelectric point
if you put a protein in a solution that is more acidic than the isolelectric point those hydrogen ions in excess will
change the carboylic acid groups that are charged to non charged, making a cation
if you put a protien in a solution that is more basic than the isoelectric point,
those amino groups will be negated, making an anion
albumin has a pi of
gamma globs have a pi of
fuzzy bands can be tightened by
increasing the ionic strength
decreasin gthe ionic strength
helps seperation
increasing ionic strength causes you to increase
the current, the heat, and heat is teh enemy
heat is generated and condesnsation occurs on the lid of the electrophoresis lid, that ccondensation is comming from th ebuffer and the gell. this is called
wick flow
heat in electrophoresis is a multiple of
the voltage current and time
polytacrylamide gell is
mainly used in research, because acrylamide is a neurotoxin, this also helps seperate by size,
ideal conditions for electrophoresis are
matrix with little endosmosis, low voltage, low ionic strength, constant current, ans short running time
what are teh general stains most commonly used to visualize proteins in electrophoresis
amido black, coomassie blue, ponceau S, and bromphenol blue
if you are interested in proteins that have lipids, you want to use what stains
oil red o, sudan black B
what else can you use to stian ur electrophoresis other than a stain or a lipid
an enzyme such as keritinkinase
works by exposing the band to a light source, the light source is going to generate a peak that is going to be high and broad depending on the density of the band.
uses high voltage and greater heat, which means it has ato have a colloing mechanism
capillary electrophoresis
albumin is always on the ____ side of the application point
if a protein migrates faster than albumin it is called
pre albumin or transtheyretin
pre albumin is ____ in liver disease
transtheretin does what
it is a protein that binds thyroxin a thoyroid hormon and retinol (vitamin a)
pre albumin is what kind of protein
an acute phase protein, these are proteins the liver makes in response to acute inflammation
pre albumin will be ____ in manluntrition
the half life for prealbumin is
2 days
it is particularly helpful for nutritional assesment in nursing homes where patients are bed ridden
we can use what to rule out inflamation
prealbumin along with c-reactive protein
c-reactive protien is
an acute phase protein
in an acute phase reaction prealbumin is
the referange range for prealbumin is
a person who is at no risk of malnutrition will have an albumin concentration ___ and a pre albumin concentraton ____
a person who is at no risk will have an albumin concentration greater than 3.2g/dL and pre albumin greater than 17mg/dL
a moderate risk of malnutrition shows a
slight decrease in both albumin g/dL and pre albumin g/dL, so 10-70 mg/dL prealbumin, and 2.5-3.2
a person with severe malnutrition will have an albumin and pre albumin of
a person with a severe risk of malnutrition will have albumin less than 2.5 g/dL and prealbumin less than 10 mg/dL
albumin does what
it maintains teh water balance between the circulatory system and the tissue
oncotic refers to
oncotic refers to the water pressure in the blood and tissues
albumin transports
ions and pigments such as heme
in nephrotic syndrome you will have large amounts of ____ lost in the urine
if the albumin is decreased in the vascular space it will become ___ and the tissue will become ____
if the albumin is decreased in the vascular space it will become hypotonic and the tissue will become hypertonic
is used around the world to quantify albumin, lipemia interfers
bromcresol green/purple
what is the normal albumin to globulin ratio
the normal alumin to globulin ratio is 1.5:1 up to 3:1
if a patients have a hypoalbuminia it will
decrease the albumin and show a decreased albumin to globulin ratio
the reference range for alpha 1 antitrypsin is
93-224 mg/dL
alpha 1 antytripsin is a
protease inhibitor
alpha 1 antitrypsin inhibits activity of
trypsin, elastase, urokinase, plasmin, thrombin, and wbc protease
alpha 1 antitrypsin is increased in
inflammation and pregnancy
alpha 1 antitrypsin is decreased in
emphysema, hyaline membrane disease, and cirrhosis
alpha 1 liporotein is a
high density lipoprotein that transports cholesterol and triglyceride
the reference range for alpha 1 liporotein is
there is none
alpha 1 lipoprotein is decreased in
tangiers disease, obstructive jaundice, diabetes mellitus
alpha 1 lipoprotein is a hihgdensity lipoprotein alsko known as
good cholesterol
the function of HDL is to
transport triglycerol
disease wheere hdl is decreased and associated with the inability of the liver to produce the alpha 1 protein used to make that lipid packet
tangiers disease
the recommendation is that the HDL concentration is greater than
alpha 1 fetoprotein concneetration in newborns is ___ and decreases to less than ____ 0.0001mg/dL
1-40mg/dL and
alpha 1 fetoprotein is going to be increased in
hepatomas, pergancy and open neural tube defect
alpha 1 carcinoembryonic antigen is a
tumor marker and normal fetal gut proetin
alpha 1 carcinoembryonic antigen is going to be increased in
70-90% of GI cancers
what is the duty of hapto globin, the alpha 2 globulin
haptoglobin gets the duty to combine free homglobin to make it soluble and form a stable complex
the reference range for alpha 2 haptoglobin is
40-180 mg Hgb bount per 100 mL serum
hapto globin is a ____ _____ protein
haptoglobin is an acute phase protein
haptoglobin is decreased in
liver diseases, and hemolytic anemia
haptoglobin is increased in i
inflammation, nephrotic syndrome
this protein is increased in nephrotic syndrome,, and this protein is decreased in nephrotic syndrome
albumin is decreased in nephrotic syndrome, haptoglobin is increased in nephrotic syndrome
alpha 2 macroglobin has amidrange concentration of
150-350 mg/dL
alpha 2 macroglobin is a
protease inhibitor
alpha 2 macroglobin is increased in
nephroic syn drome
alpha 2 macroglobulin is decreased in
liver disease and diabetes mellitus
alpha 2 ceruloplasmin does what
behaves as an oxidase, is considered an enzyme, and is a copper binding molecule than can bind 6 copper atoms
in wilsons desease what protein is decreased
alpha 2 ceruloplasmin
it is a genetic problem where the liver cannot make ceruloplasmin, which will make copper levels increase
wilsons disease
alpha 2 ceruloplasmin is decreased in
nephrotic syndrome, and wilsons disease
alpha 2 ceruloplasmin is increased in
acute phase reactions
alpha 2 liporotien is
very low density liprotein, it is a pre-betaliporotein, that is 40-80% triglyceride
40-80 percent of the total content of vldl
is triglyceride
what is the recommendation for vldl
that it be less than 150 mg/dL
vldl is decreased in
liver disease
vldl is increaed in
hyperlipproteinemias type IIb, IV, and V in this case in contrast to hdl increased lvls are not healthy
transferrin is a
beta globulin tha ttransports iron in the plus 3 state
the reference range for transferrin is
200-400 mg/dL
transferin is decreased in
nephrotic, inflammation
ttransferrin will be increased in
iron deficiency anemia, the liver will increas this in cases of iron deficiency anemia, and it will also be increased in the third trimester of pregnancy
some insurance companies use this to monitor if a patient is at risk of because of alchohol abuse, it is a glycoprotein, of teh beta globs, it is also processed in the golgi of the liver cell to attach carbs. in alchohol abusers this carb attachment process becomes defected
these beta globulins are in very lo concentration ,they wil be active in immunological disesae and used up, these include fibrinogen
compliment facors
the reference range for complement factors are
1-15 mg/dL
the reference range for fibrinogen is
150-350 mg/dL
it is the precursor for fibrin
fibrinogen is increased in
fibrinogen is decreased in
uncommonly, and in severe liver disease, premature placental rupture
beta lipoprotein is
a low density lipprotein, that is 45% cholesterol, 25% protein
beta lipprotein is increased in
nephrotic syndrome and type II hyperlipproteinemia
beta lipprotein is decreaed in
healthy individuals, and liver disease
the recommendation for beta lipprotein is
less than 100 mg/dL
gamma globulins are the ++++ peak in normal electrophoresis
beta globlulins migrate really slowly because
rthey have a pi around 7.5, near the pH buffer
beta globulins will be located near
the application point
the gamma glob types are
IgG, M, A, D, and E
how many heavy chains are in an antibody
2 connected by disulfaide linkages
how many light chains are in a immunoglobulin
which part of the antibody binds to the antigen
the variable portion of the Fc
the major binding site for antibodies are the
variable sequences in the heavy and light chians
what are the two different kind of light chains
lambda and kappa
which antibody is in the hghest concentration
which antibody is the first response
which antibodi is associated with allergies
which antibodiu is associated with mucuous mebranes and tears
what class of antibody can cross the placental barrier
Which antibody is the biggest?
M (its apentomer
which antibody is a dimer
which antibodiesa are monomers
gamma globs are decreaed in
brutons agammmaglobulinemia, digeorges syndrome, svere combined immunodeficiency
is sex linked, associated with recurrent bacterial infections, B cells are absent, as well are plasma cells, all immunoglobs are decerased, T cells are normal
Burton's agammaglobulinemia
thymic hypoplasia, t cell deficient, vulnerable to viral fungal bacterial infections involving t and b cell cooperation
digeorge syndrome
marked decrease in both T and B cells is
severe combined immuno deficiency disease
in bruton's aggamma globulinemia which are affected males or females
plasmacytoid lymphocytes secreting IgM
waldenstroms macroglobulinemia
plasma cells producing onlly heavy chains
heavy chain disease