Proteins

Front 1

whats unique about proteins vs carbs

Back 1

carbs do not contain nitrogen or sulfur

Front 2

what does the alpha carbon mean

Back 2

the alpha carbon means there are different functional groups attached to each carbon

Front 3

the carboxy group gives acidic or basic qualities

Back 3

the carboxy gives acidic qualities, it is a proton donating group

Front 4

the amine gives acidic or basic qualities

Back 4

the amine gives basic qualities, it is a proton accepting group

Front 5

any protein that has a metal ion would be a

Back 5

metalloprotein

Front 6

any protein with a carb attached woiuld be a

Back 6

any protein with a carb attached woiuld be a glycoprotein

Front 7

amino acids are called amphoteric because

Back 7

they can have either a positive or negative charge

Front 8

do carbohydrates ever have a charge

Back 8

no

Front 9

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 _______

Back 9

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

Front 10

the charge of the protein can be changed by changing the ___ of the solution the protein is in

Back 10

pH

Front 11

we operate at a pH of

Back 11

7.35-7.45

Front 12

if you put a protien in an alkaline soln it will have a ___ charge

Back 12

if you put a protein in an alkaline solution it will have a negative charge

Front 13

if you put the protein in a acidic enviornemnt it will have a _____ charge

Back 13

if you put the protein in an acidic environment it will have a positive charge

Front 14

what is the charge of leucine

Back 14

none

Front 15

what is the polarity of leucine

Back 15

non-polar

Front 16

what is the charge of arginine

Back 16

positive

Front 17

what is the polaritiy of arginine

Back 17

polar

Front 18

what is the charge of aspartic acid

Back 18

negative

Front 19

what is the polarity of aspartic acid

Back 19

polar

Front 20

what is the polarity of serine

Back 20

polar

Front 21

what is the charge of serine

Back 21

none

Front 22

what non polar amino acid did we talk about

Back 22

leucine

Front 23

what two none charged amino acids did we talk about

Back 23

leucine and serine

Front 24

how many naturally occuring amino acids are there

Back 24

20

Front 25

what makes each amino acid unique

Back 25

the r group

Front 26

leucine contains amino acids that are not charged and not polar so it does not like

Back 26

water

Front 27

amino acids that are polar are more on the ___ of the protein vs the non polar ones who like to be on the ___,

Back 27

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

Front 28

arginine has a net positive charge at physiological pH and that makes it ___ meaning it likes to be around water

Back 28

polar

Front 29

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

Back 29

polar

Front 30

so a non polar will atract a

Back 30

non polar

Front 31

amino acids are going to react with eachother through there ___ to form a peptide bond

Back 31

individual amino acids are going to react with each other through their amine group and hydroxide to form a peptide bond

Front 32

protein synthetases are basically enzymes that __ water from amino acids, allowing for covalent peptide linkages

Back 32

remove water

Front 33

peptide bonds provide the __ structure which links the amino acids to one and another

Back 33

primary structure

Front 34

secondary structure is

Back 34

these peptide linkages attract to help fold the protein

Front 35

secondary and tertiary type of reactions are those that involve things like

Back 35

van der waals interactions and hydrogen bonds, and ionic interaction, as well as disulfide linkages

Front 36

secondary and tertiary structure is how proteins are

Back 36

arranged in 3d

Front 37

quaternary structure is

Back 37

interactions between subunits in the protein, whereas myoglobin exists as a single protein, hemoglobin is made of four globin chains

Front 38

does any protein digestion occur in the mouth?

Back 38

no

Front 39

where does protein digestion start

Back 39

in the stomach

Front 40

what is the pH of the stomach

Back 40

1-2

Front 41

pepsin is

Back 41

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

Front 42

pepsin will cleave after a ____ bond

Back 42

non polar bond

Front 43

in the small intestine enzymes coming from the ____, endopeptidases, will go to the inside of the protein and cleave

Back 43

pancreas

Front 44

endopeptidases

Back 44

will go to the inside of the protein and start cleaving, by putting back in water

Front 45

endopeptidases in the small intestine are

Back 45

trypsin and chymotrypsin

Front 46

the special enzyme to digest elastin, the protein in the skin is called

Back 46

elastase

Front 47

exopeptidases go towards the end and cleave with

Back 47

either with an a aminopeptidase or a carboxypeptidase

Front 48

where does protein absorption take place

Back 48

in the microvilli via active transport of each amino acid, polar, charged, non polar, non charged

Front 49

proteion absoprtion and idgestion occurs via the

Back 49

microvilli of the digestive tract

Front 50

what three systems are in the microvilli

Back 50

the circulatory system, the lymphatic system, and the connective tissue

Front 51

amino acids are going to be absorbed via the ____ system within the villus

Back 51

circulatory

Front 52

where are the enzymes that break down carbs

Back 52

in the brush border of the villi

Front 53

1/3 of your body protein is made from

Back 53

fibrous proteins, like colagen

Front 54

elastins are going to be found in

Back 54

arteries and tendons

Front 55

what proteins make up hair

Back 55

keratins

Front 56

myosins are in

Back 56

muscles

Front 57

fibrin in sformed from

Back 57

fibrinogen

Front 58

albumins are ___ in pure water and ___ salt concentrations

Back 58

albumins are soluble in pure water and low salt concentrations

Front 59

globulins are ___ in pure whater but ____ in salt concentrations less than ___%

Back 59

globulins are insoluble in pure water but soluble in salt solutions less than 20%

Front 60

our body has a slaine level that is

Back 60

0.85 percent

Front 61

when you talk about total protein you are talking about

Back 61

all the protein in the blood

Front 62

the units for albumin is

Back 62

g/dL

Front 63

how many proteins have been identified in plasma?

Back 63

3-5thousand

Front 64

hyperproteinemia is a

Back 64

a increase in protein concentrations, relatively as seen in dehydration, or absolutely as seen in multiple myeloma and acute phase reactions

Front 65

multiple myeloma is a cancer in the

Back 65

bone marrow

Front 66

cancerous plasma cells are making increased concentrations of either whole or fragment antibodies in

Back 66

multiple myeloma

Front 67

when you are experieincing any kind of stress, there is goin tto be a fight or flight response with or without epinephrin

Back 67

acute phase reaction

Front 68

hypoproteinemia

Back 68

is an absolute decrease or relative decrease in total protein

Front 69

is a major causing of having an absolute decrease in protein, where albumin is bein glost in gram quantities

Back 69

nephrotic syndrome

Front 70

will lead to a absolute decrease in protein because the liver is the major synthesizer of proteins found in plasma except for the immunoglobulins

Back 70

liver dysfunction

Front 71

burns will cause a ____ in patients total protein

Back 71

absolute decrease

Front 72

starvation will cause a ____ in patients total protein

Back 72

absolute decrease

Front 73

where are antibodies made

Back 73

in the bone marrow or certain parts of the spleen

Front 74

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

Back 74

kwashiorkor syndrome

Front 75

patients who have salt retention, will also mean water retention meaning you will have a _____ in total protein

Back 75

relative decrease

Front 76

what is the reference method for glucose determination

Back 76

hexokinase method

Front 77

what is the reference method for protein

Back 77

kjeldal method

Front 78

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

Back 78

kjeldahl method

Front 79

is to protein as glucose oxygenase or dehydrogenase is to glucose

Back 79

the buiret

Front 80

what is the reagent in the buiret method

Back 80

copper in the plus 2 state

Front 81

protein with at least 2 peptide bonds at an alkaline pH will react with copper to form a

Back 81

colored chelate

Front 82

the copper and protein complex in the biuret method will have a ++++ color

Back 82

blue

Front 83

is the buiret method directly proportional

Back 83

yes it is

Front 84

does the biuret method follow beers law

Back 84

yes

Front 85

what are the requirments for the buiret sample

Back 85

may not be hemolyzed, may not be lipemic, and plasma could be used but usually its serum

Front 86

whats the difference between plasma and serum

Back 86

serum does not contain fibrinogen

Front 87

how long can the total protein sample be stored and at wha ttemperature

Back 87

for a week at rt

Front 88

what is the reference range for fibrinogen

Back 88

200-400mg/dL

Front 89

when you go from laying down to standing up, what is the change in your plasma water volume

Back 89

600-700mL

Front 90

if a tourniquet is left to long on the arm, what can that do to total protein

Back 90

increase

Front 91

what will bilirubin do to total protein

Back 91

increase it

Front 92

what three methods can we use to quantify total protein

Back 92

refractive index, ultraviolet absorption at 280nm, and micromethods

Front 93

the refractive indexi of water is on the total solid scale

Back 93

1.33

Front 94

proteins in general absorp at a wavelength of

Back 94

ultraviolet 280

Front 95

is a colorimetric, directly proportional method of quantifiying total protein

Back 95

bicinchonic acid method (BCA)

Front 96

a colorimetric method using a very stable dye, that is directly proprtional to quantified protein

Back 96

coomassie blue

Front 97

is a nepholometric method for quantifying total protein

Back 97

5% sulfosalicylic acid

Front 98

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

Back 98

isoelectric point

Front 99

if you put a protein in a solution that is more acidic than the isolelectric point those hydrogen ions in excess will

Back 99

change the carboylic acid groups that are charged to non charged, making a cation

Front 100

if you put a protien in a solution that is more basic than the isoelectric point,

Back 100

those amino groups will be negated, making an anion

Front 101

albumin has a pi of

Back 101

4.6

Front 102

gamma globs have a pi of

Back 102

7.5-7.6

Front 103

fuzzy bands can be tightened by

Back 103

increasing the ionic strength

Front 104

decreasin gthe ionic strength

Back 104

helps seperation

Front 105

increasing ionic strength causes you to increase

Back 105

the current, the heat, and heat is teh enemy

Front 106

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

Back 106

wick flow

Front 107

heat in electrophoresis is a multiple of

Back 107

the voltage current and time

Front 108

polytacrylamide gell is

Back 108

mainly used in research, because acrylamide is a neurotoxin, this also helps seperate by size,

Front 109

ideal conditions for electrophoresis are

Back 109

matrix with little endosmosis, low voltage, low ionic strength, constant current, ans short running time

Front 110

what are teh general stains most commonly used to visualize proteins in electrophoresis

Back 110

amido black, coomassie blue, ponceau S, and bromphenol blue

Front 111

if you are interested in proteins that have lipids, you want to use what stains

Back 111

oil red o, sudan black B

Front 112

what else can you use to stian ur electrophoresis other than a stain or a lipid

Back 112

an enzyme such as keritinkinase

Front 113

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.

Back 113

densitometry

Front 114

uses high voltage and greater heat, which means it has ato have a colloing mechanism

Back 114

capillary electrophoresis

Front 115

albumin is always on the ____ side of the application point

Back 115

opposite

Front 116

if a protein migrates faster than albumin it is called

Back 116

pre albumin or transtheyretin

Front 117

pre albumin is ____ in liver disease

Back 117

increased

Front 118

transtheretin does what

Back 118

it is a protein that binds thyroxin a thoyroid hormon and retinol (vitamin a)

Front 119

pre albumin is what kind of protein

Back 119

an acute phase protein, these are proteins the liver makes in response to acute inflammation

Front 120

pre albumin will be ____ in manluntrition

Back 120

decreased

Front 121

the half life for prealbumin is

Back 121

2 days

Front 122

it is particularly helpful for nutritional assesment in nursing homes where patients are bed ridden

Back 122

prealbumin

Front 123

we can use what to rule out inflamation

Back 123

prealbumin along with c-reactive protein

Front 124

c-reactive protien is

Back 124

an acute phase protein

Front 125

in an acute phase reaction prealbumin is

Back 125

decreased

Front 126

the referange range for prealbumin is

Back 126

20-40mg/dL

Front 127

a person who is at no risk of malnutrition will have an albumin concentration ___ and a pre albumin concentraton ____

Back 127

a person who is at no risk will have an albumin concentration greater than 3.2g/dL and pre albumin greater than 17mg/dL

Front 128

a moderate risk of malnutrition shows a

Back 128

slight decrease in both albumin g/dL and pre albumin g/dL, so 10-70 mg/dL prealbumin, and 2.5-3.2

Front 129

a person with severe malnutrition will have an albumin and pre albumin of

Back 129

a person with a severe risk of malnutrition will have albumin less than 2.5 g/dL and prealbumin less than 10 mg/dL

Front 130

albumin does what

Back 130

it maintains teh water balance between the circulatory system and the tissue

Front 131

oncotic refers to

Back 131

oncotic refers to the water pressure in the blood and tissues

Front 132

albumin transports

Back 132

ions and pigments such as heme

Front 133

in nephrotic syndrome you will have large amounts of ____ lost in the urine

Back 133

albumin

Front 134

if the albumin is decreased in the vascular space it will become ___ and the tissue will become ____

Back 134

if the albumin is decreased in the vascular space it will become hypotonic and the tissue will become hypertonic

Front 135

is used around the world to quantify albumin, lipemia interfers

Back 135

bromcresol green/purple

Front 136

what is the normal albumin to globulin ratio

Back 136

the normal alumin to globulin ratio is 1.5:1 up to 3:1

Front 137

if a patients have a hypoalbuminia it will

Back 137

decrease the albumin and show a decreased albumin to globulin ratio

Front 138

the reference range for alpha 1 antitrypsin is

Back 138

93-224 mg/dL

Front 139

alpha 1 antytripsin is a

Back 139

protease inhibitor

Front 140

alpha 1 antitrypsin inhibits activity of

Back 140

trypsin, elastase, urokinase, plasmin, thrombin, and wbc protease

Front 141

alpha 1 antitrypsin is increased in

Back 141

inflammation and pregnancy

Front 142

alpha 1 antitrypsin is decreased in

Back 142

emphysema, hyaline membrane disease, and cirrhosis

Front 143

alpha 1 liporotein is a

Back 143

high density lipoprotein that transports cholesterol and triglyceride

Front 144

the reference range for alpha 1 liporotein is

Back 144

there is none

Front 145

alpha 1 lipoprotein is decreased in

Back 145

tangiers disease, obstructive jaundice, diabetes mellitus

Front 146

alpha 1 lipoprotein is a hihgdensity lipoprotein alsko known as

Back 146

good cholesterol

Front 147

the function of HDL is to

Back 147

transport triglycerol

Front 148

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

Back 148

tangiers disease

Front 149

the recommendation is that the HDL concentration is greater than

Back 149

40mg/dL

Front 150

alpha 1 fetoprotein concneetration in newborns is ___ and decreases to less than ____ 0.0001mg/dL

Back 150

1-40mg/dL and

Front 151

alpha 1 fetoprotein is going to be increased in

Back 151

hepatomas, pergancy and open neural tube defect

Front 152

alpha 1 carcinoembryonic antigen is a

Back 152

tumor marker and normal fetal gut proetin

Front 153

alpha 1 carcinoembryonic antigen is going to be increased in

Back 153

70-90% of GI cancers

Front 154

what is the duty of hapto globin, the alpha 2 globulin

Back 154

haptoglobin gets the duty to combine free homglobin to make it soluble and form a stable complex

Front 155

the reference range for alpha 2 haptoglobin is

Back 155

40-180 mg Hgb bount per 100 mL serum

Front 156

hapto globin is a ____ _____ protein

Back 156

haptoglobin is an acute phase protein

Front 157

haptoglobin is decreased in

Back 157

liver diseases, and hemolytic anemia

Front 158

haptoglobin is increased in i

Back 158

inflammation, nephrotic syndrome

Front 159

this protein is increased in nephrotic syndrome,, and this protein is decreased in nephrotic syndrome

Back 159

albumin is decreased in nephrotic syndrome, haptoglobin is increased in nephrotic syndrome

Front 160

alpha 2 macroglobin has amidrange concentration of

Back 160

150-350 mg/dL

Front 161

alpha 2 macroglobin is a

Back 161

protease inhibitor

Front 162

alpha 2 macroglobin is increased in

Back 162

nephroic syn drome

Front 163

alpha 2 macroglobulin is decreased in

Back 163

liver disease and diabetes mellitus

Front 164

alpha 2 ceruloplasmin does what

Back 164

behaves as an oxidase, is considered an enzyme, and is a copper binding molecule than can bind 6 copper atoms

Front 165

in wilsons desease what protein is decreased

Back 165

alpha 2 ceruloplasmin

Front 166

it is a genetic problem where the liver cannot make ceruloplasmin, which will make copper levels increase

Back 166

wilsons disease

Front 167

alpha 2 ceruloplasmin is decreased in

Back 167

nephrotic syndrome, and wilsons disease

Front 168

alpha 2 ceruloplasmin is increased in

Back 168

acute phase reactions

Front 169

alpha 2 liporotien is

Back 169

very low density liprotein, it is a pre-betaliporotein, that is 40-80% triglyceride

Front 170

40-80 percent of the total content of vldl

Back 170

is triglyceride

Front 171

what is the recommendation for vldl

Back 171

that it be less than 150 mg/dL

Front 172

vldl is decreased in

Back 172

liver disease

Front 173

vldl is increaed in

Back 173

hyperlipproteinemias type IIb, IV, and V in this case in contrast to hdl increased lvls are not healthy

Front 174

transferrin is a

Back 174

beta globulin tha ttransports iron in the plus 3 state

Front 175

the reference range for transferrin is

Back 175

200-400 mg/dL

Front 176

transferin is decreased in

Back 176

nephrotic, inflammation

Front 177

ttransferrin will be increased in

Back 177

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

Front 178

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

Back 178

transferrin

Front 179

these beta globulins are in very lo concentration ,they wil be active in immunological disesae and used up, these include fibrinogen

Back 179

compliment facors

Front 180

the reference range for complement factors are

Back 180

1-15 mg/dL

Front 181

the reference range for fibrinogen is

Back 181

150-350 mg/dL

Front 182

it is the precursor for fibrin

Back 182

fibrinogen

Front 183

fibrinogen is increased in

Back 183

inflammation

Front 184

fibrinogen is decreased in

Back 184

uncommonly, and in severe liver disease, premature placental rupture

Front 185

beta lipoprotein is

Back 185

a low density lipprotein, that is 45% cholesterol, 25% protein

Front 186

beta lipprotein is increased in

Back 186

nephrotic syndrome and type II hyperlipproteinemia

Front 187

beta lipprotein is decreaed in

Back 187

healthy individuals, and liver disease

Front 188

the recommendation for beta lipprotein is

Back 188

less than 100 mg/dL

Front 189

gamma globulins are the ++++ peak in normal electrophoresis

Back 189

fifth

Front 190

beta globlulins migrate really slowly because

Back 190

rthey have a pi around 7.5, near the pH buffer

Front 191

beta globulins will be located near

Back 191

the application point

Front 192

the gamma glob types are

Back 192

IgG, M, A, D, and E

Front 193

how many heavy chains are in an antibody

Back 193

2 connected by disulfaide linkages

Front 194

how many light chains are in a immunoglobulin

Back 194

2

Front 195

which part of the antibody binds to the antigen

Back 195

the variable portion of the Fc

Front 196

the major binding site for antibodies are the

Back 196

variable sequences in the heavy and light chians

Front 197

what are the two different kind of light chains

Back 197

lambda and kappa

Front 198

which antibody is in the hghest concentration

Back 198

gamma

Front 199

which antibody is the first response

Back 199

mue

Front 200

which antibodi is associated with allergies

Back 200

IgE

Front 201

which antibodiu is associated with mucuous mebranes and tears

Back 201

A

Front 202

what class of antibody can cross the placental barrier

Back 202

IgG

Front 203

Which antibody is the biggest?

Back 203

M (its apentomer

Front 204

which antibody is a dimer

Back 204

A

Front 205

which antibodiesa are monomers

Back 205

IgD,E,G

Front 206

gamma globs are decreaed in

Back 206

brutons agammmaglobulinemia, digeorges syndrome, svere combined immunodeficiency

Front 207

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

Back 207

Burton's agammaglobulinemia

Front 208

thymic hypoplasia, t cell deficient, vulnerable to viral fungal bacterial infections involving t and b cell cooperation

Back 208

digeorge syndrome

Front 209

marked decrease in both T and B cells is

Back 209

severe combined immuno deficiency disease

Front 210

in bruton's aggamma globulinemia which are affected males or females

Back 210

males

Front 211

plasmacytoid lymphocytes secreting IgM

Back 211

waldenstroms macroglobulinemia

Front 212

plasma cells producing onlly heavy chains

Back 212

heavy chain disease