digestive system Maccromolecules Flashcards

1
Q

what are the main chemicals of life

A

vitamins/minerals
water
lipids
proteins
carbohydrates

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2
Q

what do vitamins/ minerals do in body

A

help in chemical reactions building body components

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3
Q

what does water do in body

A

helps transport and breakdown other nutrients

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4
Q

what do lipids do in the body

A

energy storage and a componet in cell membrane

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5
Q

what do proteins and nucleic acids do in the body

A

components of cell and made up amino acids

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6
Q

what do carbohydrates do in the body (main fuction)

A

primary energy source

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7
Q

what are carbohydrates composed of

A

composed of sugar carbon, hydrogen and oxygen atoms

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8
Q

what are carbohydrates 3 categorys

A

monosaccharids
disaccharids
polysaccharids

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9
Q

what are the 3 monosaccharid types

A
  • glucose
    -fructose
    -glactose
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10
Q

what are monosaccharids reffered to as

A

simple sugars or reducing sugars

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11
Q

what are the 3 types of disaccharides

A

-sucrose
-maltose
-lactose

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12
Q

definiton of disaccharides

A

two simple sugars (monosaccharides) combined together

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13
Q

what is sucrose made out of

A

gloucose and fructose

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14
Q

what is maltose made out of

A

2 glucose

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15
Q

what is lactose made out of

A

glucose and galactose

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15
Q

what process hepls form polysaccharides and disaccharides

A

dehydration syntheis

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16
Q

what is the definition of polysaccharieds

A

many simple sugars comined also by dehydration synthis

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17
Q

what ar the 3 types of polysaccharies

A

starch
cellulose
glyogen

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18
Q

what does starch do

A

stores energy in plants

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19
Q

what does cellulose do

A

carbohydrates that provide structure support in cell wall (fiber)

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20
Q

what does glycogen do

A

carbohydrate for energy in animal cells

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21
Q

what do simple carbs do

A

they’re quick fuel and makes blood glucose and inslin levels higher and let of energy quicker so less full over time

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22
Q

what do complex carbs do

A

they take more time to break down so it makes you full for longer and more energy over time

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23
Q

what is dehydration sythesis

A

processs latger molecules made from smaller by taking out the h2o and so a new bond is formed making it bigger

small to large

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24
Q

what is hydrolysis

A

when a larger molecule breaks down into smaller molecules by adding water

large to small

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25
Q

what test can you do to test if something is a monosaccharide

A

using a benedict solution test
if blue its not if yellow low red is high

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26
Q

what test is used to identify starches

A

using the iodine test to find starches (polysaccharides) is black its positive

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27
Q

what are the 3 types of lipids

A

fats
oils
wax

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28
Q

description of fats

A

lipids that are solid at room temp and is a animal source

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29
Q

description of oils

A

lipids that are liquids at room temp plant source

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30
Q

description of waxes

A

long chain lipids (cant digest)

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31
Q

what are trigylcerides made out of

A

glycerol and 3 fatty acids

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32
Q

are triglycerides polar or non-polar

A

nonpolar

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33
Q

what do trigycerides do

A

they float through the blood and used to store energy for later

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34
Q

what are phospholipids made out of

A

phosphate and glyerol bonded 2 fatty acids

has hydrophopic tails
hydrophillic heads

35
Q

what are lipids function

A

-long term energy storage
- cell memberanes
- carries vitamins

36
Q

when theres a sequence of amino acids what does it form

A

polypeptide chain

37
Q

what are traits of the primary protein structure

A

its very dissorginized

string of amino acids come together called polypeptieds

38
Q

what are the 4 types of peptides

A
  • vasopressin
    -oxytocin
  • angiotensins
  • defensins
39
Q

traits of the protein secondaty structure do

A

folding of the polypeptide backbones and 2 possible shapes (beta or alpha)

form from hydo bonding

40
Q

traits of protein teritary structure

A

folds into 3 dimentional shapes folding the entire polypeptide chain happens from th R groups influence

41
Q

what are the protein teritary structure influences (how they bond and form)

A
  • hydro bonds
  • ionic bonds
    -london forces
    -hydrophbic on non-polor sides
42
Q

traits protein quaternary structure

A

multiple polypeptide chains

ex hemoglobin

has chain intractions to make shape

43
Q

what does denaturation mean

A
  • causes temporary change to shape on protein

-happens from heat, radiation, or diff ph

44
Q

what does coagulation mean

A

it can occur after denaturation and is a permanent change in protein shape (like blood clot)

45
Q

vasopressin peptide fuction

A

regulate water in surrounding cells

46
Q

oxytocin peptide function

A

create feeling of love and bonding

47
Q

defensins peptide function

A

help with wound healthing

48
Q

angiotenins peptide function

A

regulate blood pressure

49
Q

Catalyst function

A

help chemical reactions (breaking down nutrients)

because it lowers activation energy so the reaction can happen quicker without as much energy going in

50
Q

Active Site on an enzyme function

A

area on enzyme where reaction takes place

51
Q

Substrate function

A

a molecule that an enzyme works on (thing that fits into the active site)

52
Q

when something has the ending ase what does it mean it is

A

an enzyme

52
Q

what 2 things are an enyme under carbohydrase (breaking down carbs)

A

Amylase (salivary, pancreatic),
Disaccharidase (maltase, lactase)

52
Q

what 2 things are an enyme under Protease (breakdown proteins)

A

Pepsin, trypsin, erepsin

52
Q

what 2 things are an enyme under Lipase (breakdown lipids)

A

Lipase and Phospholipase

53
Q

what are the steps to enzymes

A

1) Enzyme’s active site binds the substrate molecule(s)

2) Chemical reaction takes place

3) Product is released and enzyme is ready to work again

54
Q

what do Cofactors / Coenzymes do

A

help enzymes bind to substrate

55
Q

whats the difference between Cofactors / Coenzymes

A

Cofactor = inorganic ion (Fe, Zn, K)
Coenzyme = organic molecule from a vitamin

56
Q

what are factors that affect enzymes reactions

A

pH
Substrate Concentration
Temperature
Competitive Inhibition
Regulation of Enzyme Activity (feedback)

57
Q

substrate is the substance you are..

A

breaking down

58
Q

whats Competitive Inhibition

A

Attaches to the active site, preventing the enzyme from working

ex penicilin

59
Q

Feedback Inhibition

A

regulation of chemicals is essential - if we have enough testosterone, we wouldn’t want excess as this could cause heart problems

(regulates how much chemicals)
(called negative bc slows down chemicicals there)

60
Q

Allosteric Activity

A

a change in an enzyme caused by a binding of a molecule

61
Q

Precursor Activity

A

when substrate accumulates it binds to the regulatory site improving fit of the active site,

speeding up the formation of products
(possitive bc more )

62
Q

what does salivary amylase do

A

made from mouths salivary glands breaks down startch to shorter polysaccharids

63
Q

where are disaccharids made / act

A

made in small intestine and act there

64
Q

what do disaccharids do

A

breaks down disaccharids to monosaccharids

65
Q

what does pancreatic amylase do

A

breaks down polysaccharide chains into disaccharides from pancrease to act in small intestine

66
Q

what are the steps of carb enzyme break down

A

foods chewed up
then salivary glands activated and breakes down starches to poly

then after food travels w peristalsis stomach has contractions

small intestine gets food from stomach pancrease secreates pancreatic amylase into small intestine to break poly to di

then disaccharids secreated from small intestine to break di to mono

67
Q

where does lipid digestion take place

A
  • small intestine, liver, pancrease
68
Q

what enzyme is made in liver and helps with lipid digestion

A

bile is made liver stored in gallbladder and it is used to emulsify / break large to small

(also increases sa while doing so )

69
Q

what happens in the small intesine when any food enters lipid digestion

A

when any food enters small intestine it releases hormones and gallbladder will secreate bile
pancrease secreates lipase and phpsphipase

70
Q

what does lipase do

A

produced in pancrease acts in small intestine breaks down fat into gycerol/fatty acids

71
Q

how is cck activated and how it activates bile / how does it act

A
  • activated when fat enters small i and stimulates release cck
  • cck carried by bloodstream to gallbladder then there it realeases bile from gallbadder

-bile emulsifys fat

72
Q

where does protein digestion occur

A

stomach
small intestine
pancrease

73
Q

what does the stomach stimulate to release more hcl

A

gastrin helps release more hcl

74
Q

how is pepsin made in protein digestion

A

once gastrin released that makes more hcl that reacts with pepsinogen to create pepsin

75
Q

what does pepsin do in protein disestion

A

it starts chemical breakdown proteins polypeptide chains to shorter ones

76
Q

where does protein digestion start

A

stomach

77
Q

what happens in the small intestine with protein digestion

A

trypsinogen is converted to be typsin from pancrease that continues to digest already working on the partially digested

and erepsin made from pancrease finishes break off of proteins making them individual amino acids

78
Q

where is typsin and erepsin made

A

pancrease then they act in small intestine

79
Q

what is the part of the large intestine that absobes water

A

colon

80
Q

what is the ending section on the small intestine where most digestion occurs

A

caecum

81
Q

what are folds on stomach called

A

rugae