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212 Cards in this Set
- Front
- Back
whats unique about proteins vs carbs
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carbs do not contain nitrogen or sulfur
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what does the alpha carbon mean
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the alpha carbon means there are different functional groups attached to each carbon
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the carboxy group gives acidic or basic qualities
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the carboxy gives acidic qualities, it is a proton donating group
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the amine gives acidic or basic qualities
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the amine gives basic qualities, it is a proton accepting group
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any protein that has a metal ion would be a
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metalloprotein
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any protein with a carb attached woiuld be a
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any protein with a carb attached woiuld be a glycoprotein
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amino acids are called amphoteric because
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they can have either a positive or negative charge
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do carbohydrates ever have a charge
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no
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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 _______
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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
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the charge of the protein can be changed by changing the ___ of the solution the protein is in
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pH
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we operate at a pH of
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7.35-7.45
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if you put a protien in an alkaline soln it will have a ___ charge
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if you put a protein in an alkaline solution it will have a negative charge
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if you put the protein in a acidic enviornemnt it will have a _____ charge
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if you put the protein in an acidic environment it will have a positive charge
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what is the charge of leucine
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none
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what is the polarity of leucine
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non-polar
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what is the charge of arginine
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positive
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what is the polaritiy of arginine
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polar
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what is the charge of aspartic acid
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negative
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what is the polarity of aspartic acid
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polar
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what is the polarity of serine
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polar
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what is the charge of serine
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none
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what non polar amino acid did we talk about
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leucine
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what two none charged amino acids did we talk about
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leucine and serine
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how many naturally occuring amino acids are there
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20
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what makes each amino acid unique
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the r group
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leucine contains amino acids that are not charged and not polar so it does not like
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water
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amino acids that are polar are more on the ___ of the protein vs the non polar ones who like to be on the ___,
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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
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arginine has a net positive charge at physiological pH and that makes it ___ meaning it likes to be around water
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polar
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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
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polar
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so a non polar will atract a
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non polar
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amino acids are going to react with eachother through there ___ to form a peptide bond
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individual amino acids are going to react with each other through their amine group and hydroxide to form a peptide bond
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protein synthetases are basically enzymes that __ water from amino acids, allowing for covalent peptide linkages
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remove water
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peptide bonds provide the __ structure which links the amino acids to one and another
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primary structure
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secondary structure is
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these peptide linkages attract to help fold the protein
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secondary and tertiary type of reactions are those that involve things like
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van der waals interactions and hydrogen bonds, and ionic interaction, as well as disulfide linkages
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secondary and tertiary structure is how proteins are
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arranged in 3d
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quaternary structure is
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interactions between subunits in the protein, whereas myoglobin exists as a single protein, hemoglobin is made of four globin chains
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does any protein digestion occur in the mouth?
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no
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where does protein digestion start
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in the stomach
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what is the pH of the stomach
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1-2
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pepsin is
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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
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pepsin will cleave after a ____ bond
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non polar bond
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in the small intestine enzymes coming from the ____, endopeptidases, will go to the inside of the protein and cleave
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pancreas
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endopeptidases
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will go to the inside of the protein and start cleaving, by putting back in water
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endopeptidases in the small intestine are
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trypsin and chymotrypsin
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the special enzyme to digest elastin, the protein in the skin is called
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elastase
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exopeptidases go towards the end and cleave with
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either with an a aminopeptidase or a carboxypeptidase
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where does protein absorption take place
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in the microvilli via active transport of each amino acid, polar, charged, non polar, non charged
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proteion absoprtion and idgestion occurs via the
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microvilli of the digestive tract
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what three systems are in the microvilli
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the circulatory system, the lymphatic system, and the connective tissue
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amino acids are going to be absorbed via the ____ system within the villus
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circulatory
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where are the enzymes that break down carbs
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in the brush border of the villi
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1/3 of your body protein is made from
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fibrous proteins, like colagen
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elastins are going to be found in
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arteries and tendons
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what proteins make up hair
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keratins
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myosins are in
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muscles
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fibrin in sformed from
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fibrinogen
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albumins are ___ in pure water and ___ salt concentrations
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albumins are soluble in pure water and low salt concentrations
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globulins are ___ in pure whater but ____ in salt concentrations less than ___%
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globulins are insoluble in pure water but soluble in salt solutions less than 20%
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our body has a slaine level that is
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0.85 percent
|
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when you talk about total protein you are talking about
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all the protein in the blood
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the units for albumin is
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g/dL
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how many proteins have been identified in plasma?
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3-5thousand
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hyperproteinemia is a
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a increase in protein concentrations, relatively as seen in dehydration, or absolutely as seen in multiple myeloma and acute phase reactions
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multiple myeloma is a cancer in the
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bone marrow
|
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cancerous plasma cells are making increased concentrations of either whole or fragment antibodies in
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multiple myeloma
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when you are experieincing any kind of stress, there is goin tto be a fight or flight response with or without epinephrin
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acute phase reaction
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hypoproteinemia
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is an absolute decrease or relative decrease in total protein
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is a major causing of having an absolute decrease in protein, where albumin is bein glost in gram quantities
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nephrotic syndrome
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will lead to a absolute decrease in protein because the liver is the major synthesizer of proteins found in plasma except for the immunoglobulins
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liver dysfunction
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burns will cause a ____ in patients total protein
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absolute decrease
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starvation will cause a ____ in patients total protein
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absolute decrease
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where are antibodies made
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in the bone marrow or certain parts of the spleen
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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
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kwashiorkor syndrome
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patients who have salt retention, will also mean water retention meaning you will have a _____ in total protein
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relative decrease
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what is the reference method for glucose determination
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hexokinase method
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what is the reference method for protein
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kjeldal method
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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
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kjeldahl method
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is to protein as glucose oxygenase or dehydrogenase is to glucose
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the buiret
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what is the reagent in the buiret method
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copper in the plus 2 state
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protein with at least 2 peptide bonds at an alkaline pH will react with copper to form a
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colored chelate
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the copper and protein complex in the biuret method will have a ++++ color
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blue
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is the buiret method directly proportional
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yes it is
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does the biuret method follow beers law
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yes
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what are the requirments for the buiret sample
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may not be hemolyzed, may not be lipemic, and plasma could be used but usually its serum
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whats the difference between plasma and serum
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serum does not contain fibrinogen
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how long can the total protein sample be stored and at wha ttemperature
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for a week at rt
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what is the reference range for fibrinogen
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200-400mg/dL
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when you go from laying down to standing up, what is the change in your plasma water volume
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600-700mL
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if a tourniquet is left to long on the arm, what can that do to total protein
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increase
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what will bilirubin do to total protein
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increase it
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what three methods can we use to quantify total protein
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refractive index, ultraviolet absorption at 280nm, and micromethods
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the refractive indexi of water is on the total solid scale
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1.33
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proteins in general absorp at a wavelength of
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ultraviolet 280
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is a colorimetric, directly proportional method of quantifiying total protein
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bicinchonic acid method (BCA)
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a colorimetric method using a very stable dye, that is directly proprtional to quantified protein
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coomassie blue
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is a nepholometric method for quantifying total protein
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5% sulfosalicylic acid
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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
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isoelectric point
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if you put a protein in a solution that is more acidic than the isolelectric point those hydrogen ions in excess will
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change the carboylic acid groups that are charged to non charged, making a cation
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if you put a protien in a solution that is more basic than the isoelectric point,
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those amino groups will be negated, making an anion
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albumin has a pi of
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4.6
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gamma globs have a pi of
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7.5-7.6
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fuzzy bands can be tightened by
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increasing the ionic strength
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decreasin gthe ionic strength
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helps seperation
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increasing ionic strength causes you to increase
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the current, the heat, and heat is teh enemy
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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
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wick flow
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heat in electrophoresis is a multiple of
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the voltage current and time
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polytacrylamide gell is
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mainly used in research, because acrylamide is a neurotoxin, this also helps seperate by size,
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ideal conditions for electrophoresis are
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matrix with little endosmosis, low voltage, low ionic strength, constant current, ans short running time
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what are teh general stains most commonly used to visualize proteins in electrophoresis
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amido black, coomassie blue, ponceau S, and bromphenol blue
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if you are interested in proteins that have lipids, you want to use what stains
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oil red o, sudan black B
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what else can you use to stian ur electrophoresis other than a stain or a lipid
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an enzyme such as keritinkinase
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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.
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densitometry
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uses high voltage and greater heat, which means it has ato have a colloing mechanism
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capillary electrophoresis
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albumin is always on the ____ side of the application point
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opposite
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if a protein migrates faster than albumin it is called
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pre albumin or transtheyretin
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pre albumin is ____ in liver disease
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increased
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transtheretin does what
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it is a protein that binds thyroxin a thoyroid hormon and retinol (vitamin a)
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pre albumin is what kind of protein
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an acute phase protein, these are proteins the liver makes in response to acute inflammation
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pre albumin will be ____ in manluntrition
|
decreased
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the half life for prealbumin is
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2 days
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it is particularly helpful for nutritional assesment in nursing homes where patients are bed ridden
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prealbumin
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we can use what to rule out inflamation
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prealbumin along with c-reactive protein
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c-reactive protien is
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an acute phase protein
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in an acute phase reaction prealbumin is
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decreased
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the referange range for prealbumin is
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20-40mg/dL
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a person who is at no risk of malnutrition will have an albumin concentration ___ and a pre albumin concentraton ____
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a person who is at no risk will have an albumin concentration greater than 3.2g/dL and pre albumin greater than 17mg/dL
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a moderate risk of malnutrition shows a
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slight decrease in both albumin g/dL and pre albumin g/dL, so 10-70 mg/dL prealbumin, and 2.5-3.2
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a person with severe malnutrition will have an albumin and pre albumin of
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a person with a severe risk of malnutrition will have albumin less than 2.5 g/dL and prealbumin less than 10 mg/dL
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albumin does what
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it maintains teh water balance between the circulatory system and the tissue
|
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oncotic refers to
|
oncotic refers to the water pressure in the blood and tissues
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albumin transports
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ions and pigments such as heme
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in nephrotic syndrome you will have large amounts of ____ lost in the urine
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albumin
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if the albumin is decreased in the vascular space it will become ___ and the tissue will become ____
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if the albumin is decreased in the vascular space it will become hypotonic and the tissue will become hypertonic
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is used around the world to quantify albumin, lipemia interfers
|
bromcresol green/purple
|
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what is the normal albumin to globulin ratio
|
the normal alumin to globulin ratio is 1.5:1 up to 3:1
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if a patients have a hypoalbuminia it will
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decrease the albumin and show a decreased albumin to globulin ratio
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the reference range for alpha 1 antitrypsin is
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93-224 mg/dL
|
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alpha 1 antytripsin is a
|
protease inhibitor
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alpha 1 antitrypsin inhibits activity of
|
trypsin, elastase, urokinase, plasmin, thrombin, and wbc protease
|
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alpha 1 antitrypsin is increased in
|
inflammation and pregnancy
|
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alpha 1 antitrypsin is decreased in
|
emphysema, hyaline membrane disease, and cirrhosis
|
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alpha 1 liporotein is a
|
high density lipoprotein that transports cholesterol and triglyceride
|
|
the reference range for alpha 1 liporotein is
|
there is none
|
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alpha 1 lipoprotein is decreased in
|
tangiers disease, obstructive jaundice, diabetes mellitus
|
|
alpha 1 lipoprotein is a hihgdensity lipoprotein alsko known as
|
good cholesterol
|
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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
|
40mg/dL
|
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alpha 1 fetoprotein concneetration in newborns is ___ and decreases to less than ____ 0.0001mg/dL
|
1-40mg/dL and
|
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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
|
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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
|
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hapto globin is a ____ _____ protein
|
haptoglobin is an acute phase protein
|
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haptoglobin is decreased in
|
liver diseases, and hemolytic anemia
|
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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
|
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alpha 2 macroglobin has amidrange concentration of
|
150-350 mg/dL
|
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alpha 2 macroglobin is a
|
protease inhibitor
|
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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
|
transferrin
|
|
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
|
|
fibrinogen is increased in
|
inflammation
|
|
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
|
fifth
|
|
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
|
2
|
|
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
|
gamma
|
|
which antibody is the first response
|
mue
|
|
which antibodi is associated with allergies
|
IgE
|
|
which antibodiu is associated with mucuous mebranes and tears
|
A
|
|
what class of antibody can cross the placental barrier
|
IgG
|
|
Which antibody is the biggest?
|
M (its apentomer
|
|
which antibody is a dimer
|
A
|
|
which antibodiesa are monomers
|
IgD,E,G
|
|
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
|
males
|
|
plasmacytoid lymphocytes secreting IgM
|
waldenstroms macroglobulinemia
|
|
plasma cells producing onlly heavy chains
|
heavy chain disease
|