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Biology 20 IB > D1 A. Digestive System > Flashcards

D1 A. Digestive System Flashcards

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1
Q

Nutrient

A

A substance that provides nourishment essential for growth and the maintenance of life

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2
Q

Essential Nutrients

A
  • Carbohydrates (sugar)
  • Lipids (fats)
  • Proteins
  • Vitamins
  • Minerals
  • Nucleic Acids

Water is not a nutrient even though its essential for life

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3
Q

True or False

Starch is a type of carbohydrate

A

True

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4
Q

True or False

When fats are digested, amino acids are formed

A

False

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5
Q

True or False

Enzymes speed up the rate of digestion

A

True

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6
Q

True or False

The large intestine is longer than the small intestine

A

False

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7
Q

True or False

Proteins are made up of amino acids

A

True

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8
Q

True or False

Proteins are our main source of energy

A

False

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9
Q

Dehydration Synthesis Reaction

A
  • The creation of larger molecules from smaller monomers
  • Water is released
  • Also known as condensation reaction
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10
Q

Hydrolysis Reaction

A
  • A chemical reaction where water molecules break larger molecules (polymers) into smaller ones (monomers)
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11
Q

Metabolism

A

The totality of chemical reaction that occur in a cell/organism

  • Provide energy
  • Enable synthesis to make new materials
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12
Q

Anabolism

A

Anabolic reactions build up complex molecules from simple ones

  • Formation of macromolecules from monomers
  • Condensation reactions
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13
Q

Catabolism

A
  • Breaks complex molecules into simpler ones
  • Releases monomers
  • Hydrolysis reactions
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14
Q

Organic Compounds

A
  • Carbon-containing molecules
    Exceptions: Carbonate and oxides of carbon such as carbon dixoide
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15
Q

Carbohydrates

A
  • Fast energy nutrient
  • Largest component in most diets
  • Get these from plants → cannot produce them ourselves
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16
Q

Carbohydrate Structure

A
  • Single sugar (monomers) or chain of many sugar units (polymers)
  • Classified by the number of sugars they contain
  • Chemical Formula: Usually at a ratio of 1C: 2H : 1O
  • “ose” suffix
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17
Q

Monosaccharides

A
  • Simple sugar (single sugar units); one sugar ring
  • 3-6 carbons

* Glucose
* Fructose
* Galactose

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18
Q

Isomers

A
  • Same chemical formula, but different arrangements of atoms
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19
Q

Disaccharides

A
  • 2 sugar rings / monosaccharides together
  • Formed via dehydration synthesis
  • Water molecule is formed from 2 monosaccharides
  • Glycosidic bond is formed
  • Break disaccharide bond via hydrolysis (opposite)
  • Water molecule is used to break bond

  • Maltose: 2 sugar units
  • Sucrose: 1 glucose + 1 fructose
  • Lactose: 1 glucose + 1 galactose
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20
Q

Polysaccharides

A
  • Carbohydrates fromed from many monosaccharide subunits
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21
Q

Polysaccharides

Cellulose

A
  • Cellulose: Polysaccharide that makes up plant cell walls (glucose)
  • Different bonding that starch and glycogen
  • Composed of B-glucose subunits (linear arrangement)
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22
Q

Polysaccharides

Glycogen

A
  • Glycogen: polysaccharides used in animals to store carbs (glucose)
  • Energy storage in humans and animals
  • Composed of a-glucose subunits (branched orientation)
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23
Q

Polysaccharides

Starch

A
  • Starch: Energy storage used in plabnts. Exists in form of amylose or amylopectin
  • Amylose: 1000 or more glucose subunits; unbranched polymer of glucose
  • Composed of a-glucose subunits (linear)
  • Amylopectin: 1000-6000 glucose subunits
  • Composed of a-glucose subunits (branched)
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24
Q

Lipid Function

A
  • Storage of energy (triglycerides)
  • Hormonal roles (e.g. steroid hormone)
  • Insulation (e.g. sphingolipids)
  • Protection of internal cavities (e.g. fats and waxes)
  • Structral components of cells (e.g. phospholipids)
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25
Q

Lipid Structure

A
  • Non-polar
  • Composed of 2 structural units; glycerol and fatty acids
  • Combined via dehydration synthesis to form an ester bond
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26
Q

Triglycerides

A
  • Long-term energy source
  • Glycerol + 3 fatty acids
  • Removal of water during synthesis
  • Oils: Triglycerides that are liquid at room temp
  • Unsaturated fat: Some double bonds between carbon atoms
  • 1 double bond → monounsaturated
  • 2 or more double bonds → polyunsaturated
  • Reactive; more easily broken down
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27
Q

Fatty Acids

A

Fats - Usually solid at room temperature
Saturated Fatty Acid - Only single bond between carbon atoms

  • Strong bonds; hard to break down
  • COOH is a carboxylic acid
  • It’s linear shape (14-20 carbons) makes the structure of a fatty acid an acid
  • Single bonds between carbons, double bonds between carbon and oxygen
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28
Q

Structural Isomers

Cis Isomer

A
  • H atoms are on same side
  • Double bond creates kink
  • Are loosely packed (liquid)
  • Occurs commonly in nature
  • Generally good for health
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29
Q

Structural Isomers

Trans Isomer

A
  • H atoms on different sides
  • No kink in chain is created
  • Are tightly packed (solid)
  • Common in processed food
  • Generally bad for health
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30
Q

Phospholipids

A
  • Phosphate group bonded to glycerol and 2 fatty acids
  • Negatively charged P replaces one of the fatty acids
  • Head (phosphate + glycerol): Polar end = soluble in water
  • Tail (fatty acids): Non-polar = insoluble in water
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31
Q

Waxes

A
  • Long-chain fatty acids joined to long-chain alcohols or to carbon rings
  • Insoluble in water
  • Waterproof coating on plant leaves, animal feather, fur
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32
Q

Energy Storage - Lipids vs. Carbohydrates

A

Storage

  • Carbohydrate - Short term
  • Lipid - Long term

Osmotic effect

  • Carbohydrate - More effect on cell
  • Lipid - Less effect on cell

Digestion

  • Carbohydrate - Readily digested
  • Lipid - Less easily digested

ATP yield

  • Carbohydrate - Lower (rougly half)
  • Lipid - Higher (roughly x2)

Solubility

  • Carbohydrate - Water soluble (monomers)
  • Lipids - Not water soluble
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33
Q

Body Mass Index

A

BMI = Mass in kg / (height in m)2

  • Value between 18.5 - 24.9 is healthy
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34
Q

Protein Functions

A
  1. Defense (antibodies)
  2. Movement
  3. Catalyst (enzyme)
  4. Signalling (hormone)
  5. Structure (mechanical support)
  6. Transport (carrier/channel proteins, hemoglobin)
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35
Q

What are proteins made out of

A
  • Amino acids
  • Carbon
  • Oxygen
  • Hydrogen
  • Nitrogen
  • Sulfur
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36
Q

How many differen amino acids are there

A

20:
9 ESSENTIAL, 11 NON-ESSENTIAL

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37
Q

What determines type of protein

A

Order and # of proteins

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38
Q

Polypeptide

A

Chain of amino acids

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39
Q

Protein levels of structure

Primary

A
  • Unique sequence of amino acids in the chain
  • Determines secondary structure
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40
Q

Protein levels of structure

Secondary

A
  • Formed by hydrogen bonds between peptide chains (between backbone, not R group)
  • H bond can pull chain into alpha helix and beta pleated sheets
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41
Q

Types of interactions

Hydrophobic interactions

A

These amino acids orient themselves towards the center of polypeptide to avoid the water

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42
Q

Types of interactions

Disulphide Bridge

A

The amino acid cysteine forms a bond with another cysetine through its R group

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43
Q

Types of interaction

Hydrogen Bonds

A

Polar “R” groups on the amino acids form bonds with other Polar R group

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44
Q

Types of interactions

Hydrophillic Interactions

A

These amino acids orient themselves outwards to be close to the water

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45
Q

Types of interactions

Ionic Bonds

A

Positively charged R groups bond together

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46
Q

Types of interactions

Van der Waals

A
  • Weak interactions between hydrophobic side chains
  • Increases stability
  • Responsible for folding
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47
Q

Types of interactions

Covalent Bonds

A
  • Disulfide bonds
  • Form disulfide bridge - Strong links
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48
Q

Protein levels of structure

Teriary

A
  • Depends on 1o and 2o structures
  • Additional bending/folding due to interactions between R groups of amino acids
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49
Q

Fibrous Protein

A
  • Has a structural role
  • Insoluble in water
50
Q

Globular Protein

A
  • Has a functional role
  • Soluble in water
51
Q

Protein levels of structure

Quaternary

A
  • Large, globular proteins
  • 2 or more polypeptide chains (same or different)
    2: dimer
    4: tetramer
  • Some polypeptides do not have a quaternary structure
52
Q

Why do proteins fold

A

To be more stable

53
Q

Denaturation

A

Uncoil, assume new shape = change in biological property

  • When the influencing factor is removed, the protein will assume its original shape
54
Q

2 key coniditons that can denature proteins

A
  1. Temperature - Can disrupt bonds that hold proteins together
  2. pH - Can alter charge of protein, and change its solubility/shape
55
Q

Coagulation

A

Permanent change

  • E.g. Boiling an egg = Change in protein shape
56
Q

Genome

A

All the genes of a cell, tissue, or an organism

57
Q

Proteome

A

All the proteins produced by a cell, tissue or organism

  • Individuals have a unique proteome
  • Variable because only some cells produce specific proteins
  • Human proteome = 100 000 proteins
  • Small differences in DNA = differences in proteome
58
Q

Cholestrol

A
  • Type of lipid found in cell membranes
  • Used to synthesize hormones
  • Lipoprotein = protein + lipid
  • HDL = High Density Lipoprotein (good) (bring LDL to liver to be broken down)
59
Q

Nucleic Acid

A
  • Hereditary material
  • Composed of nucleotides
60
Q

Enzymes

A
  • Most reactions are not spontaneous
  • Add thermal energy to system = increase kinetic energy = faster, more collision = more likely for reaction to occur
  • Enzymes work at low temp.
  • 3D proteins that act as catalysts
  • Increase reaction probability
  • Often end with -ase
61
Q

Catalysts

A
  • A substance that increases the rate of chemical reaction without being changed itself or become part of the product
  • Each enzyme usually controls just one reaction
62
Q

Activation Energy

A
  • The energy that must be supplied to cause a reaction
  • Enzymes lower the necessary energy of activation
63
Q

4 Steps of Enzyme Action

A
  1. Subrate binds with enzyme
  2. Enzyme undergoes confirmational change
  3. Substrates converted to products
  4. Products are relased
64
Q

Lock & Key Model

A
  • Enzymes act as keys to lock or unlock substrates
  • Substrate: Reactants in an enzymatic reaction
  • Active Site: Region on enzyme where substrates attach
65
Q

Induced Fit Model

A
  • Replaced lock and key model
  • The enzyme (active site) changes shape to fit between site and substrate
  • Increases rate of chemical reaction
65
Q

Particle Collision Theory

A
  • The frequency of collisions determines the rate of enzyme activity
  • If you increase the probability of collisions occuring, then you increase the frequency of enzyme activity
66
Q

Factors helping ezyme combine with substrate

Coenzymes

A

Molecule that assists an enzyme to complete a reaction (organic), synthesized from vitamins

67
Q

Factors helping enzyme combine with substrate

Cofactors

A

Inorganic enzyme helpers

68
Q

Factors affecting enzyme activity

Temperature

A
  • Increase temp. → increase activity, to a point
  • Too low of temp. → not enough energy for reaction to occur
  • Enzyme is denatured at high temps.
69
Q

Factors affecting enzyme activity

pH

A
  • Changing pH changes charge/solubility or shape of enzyme
  • Decreases ability to bind to the substrate
  • Optimal pH = peak enzyme activity and enzyme specificity
70
Q

Factors affecting enzyme activity

Substrate Concentration

A
  • The greater the number of substrate molecules = the greater the chance of successful collisions
  • Plateau because all active sites are occupied
71
Q

Factors affecting enzyme activity

End Product Concentration

A
  • As enzymes work, they produce an end product
  • Some are able to affect another enzymes activity and thus cause feedback inhibition
  • Some are poisonous to enzymes in high concentrations
  • The substrate can bind to the active site
  • Final product attaches to the regulatory site and changes the shape of the enzyme so the substrate cannot bind
72
Q

Factors affecting enzyme activity

Competitive Inhibitors

A
  • Molecule so close to enzyme’s substrate that it competes for the active site
  • Inhibitor binds to enzyme and will not allow product to be produced
73
Q

Factors affecting enzyme activity

Non-competitive inhibitors - allosteric activity

A
  • A chemical binds to a regulatory site causing the active site to change shape
  • Enzyme that shapes due to a chemical binding to the regulatory site = allosteric activity
  • Sometimes this can cause feedback inhibition (shut off activity)
  • Sometimes this can cause a reaction to proceed (precursor activity)
74
Q

Regulatory of Enzyme Activity - Allosteric Activity

Negative Feedback / Feedback Inhibition

A
  • Occurs when an end product can bind to an enzyme and become a noncompetitive inhibitor slowing the rate of reaction of an enzyme
75
Q

Regulatory of Enzyme Activity - Allosteric Activity

Precursor Activity

A
  • Substrate molecules accumulate → substrate molecules attach to the regulatory site of an enzyme in a pathway → improves fit between enzyme and substrate → increases reaction rate
76
Q

Digestion

A
  • Process where food is broken down into nutrients your body can use as energy
  • Beings in your mouth, finishes at the terminal ileum
77
Q

Mechanical Digestion

A

Cutting/crushing of food into smaller pieces

78
Q

Chemical Digestion

A

Breakdown of food using enzymes

79
Q

Peristalsis

A

Rhythmic muscle contraction of longitudinal muscles

  • Occurs in: Esophagus, Stomach, Intestines, Rectum
80
Q

Segmentation

A

Rhythmic muscle contractions of circular muscles. Moves food back and forth (mixes food)

81
Q

4 Main components of digestive process

A
  • Ingestion (taking in nutrients)
  • Digestion (breakdown of complex organic molecules → smaller components by enzymes)
  • Absorption (transport of digested nutrients to body cells)
  • Egestion (Removal of food waste from body)
82
Q

Roles of saliava

A
  • Contains amylase to breakdown starch
  • Lubricates mouth/throat
  • Protects teeth from cavity causing bacteria
83
Q

Oral Cavity

A
  • Salivary glands secrete saliava (begins chemical digestion)
  • Tongue determines which food needs to be further processed
  • Taste buds communicate which food needs to be processed further
  • Moves food and helps shape it into a bolus
  • When swallowing - pushes bolus to back of oral cavity and pharynx
84
Q

Esophagus

A
  • Flexible tube that leads to stomach
  • Secretes mucus
  • Passes through the diaphragm to connect with stomach at the lower esophageal sphincter which regulated entry
85
Q

Stomach

A
  • At the left side of the abdodmen
  • Secretes gastric juices
  • Stores food, continues digestion but does absorb a few compounds
  • Has a lining of a layer of mucus which protects it from being digested by pepsin
86
Q

Pyloric Sphincter

A

Moves food and stomach acid → small intestine

87
Q

Chyme

A

Ingested food and digestive juice

88
Q

Stomach - Mechanical Digestion

A

Crisscrossed muscle layers that create chruning and mixing motions

89
Q

Gastrin

A

A hormone that stimulates release of HCL

90
Q

HCL

A
  • Secreted from parietal cell
  • Can convert pepsinogen → pepsin
91
Q

Pepsin

A

Begings to hydrolyze protein into smaller polypeptides by breaking peptide bonds; works in acidic conditions

92
Q

Stomach - Peptic Ulcer

A
  • Ulcers are open sores that form in stomach/duodenum
  • When the mucus layer is reduced, stomach acid can damage the tissue
93
Q

Small Intestine

A

Responsible for:

  • Breaking down food
  • Absorbing nutrients
  • Solidifying waste

3 Sections:

  • Duodenum
  • Jejenum
  • Ileum
94
Q

Small Intestine

Duodenum

A
  • Chyme leaves the stomach and enters the duodenum
  • Low pH of chyme stimulates hormone secretion
  • Secretin causes release of NaHCo3 (sodium bicarbonate) from the pancreas
  • NAHCo3 nuetralizes gastric fluid → raising pH to 8
  • Amino acids and fatty acids in chyme releases CCK
  • CCK stimulates pancreas to release pancreatic enzymes
  • CCL stimulates gallbladder to contract and release bile
95
Q

Duodenum response to lipids

A
  • Secretes enterogastrone hormone
  • Inhibits secretion of gastric juices by stomach
  • Slows down peristalsis; causing food to move slowly
  • Thus, increased time for fat digestion
96
Q

Accessory Organs

A

Food does not pass directly through these organs, but they still contribute to digestion

  • Salivary glands
  • Pancreas
  • Liver
  • Gallbladder
97
Q

Pancreas

A

Endocrine Cells (produces hormones)

  • Insulin (decrease blood glucose)
  • Glucagon (increase blood glucose)

Exocrine Cells (produce gastric juice) - main digestive enzymes

  • Pancreatic amylase
  • Proteases
  • Pancreatic lipase
98
Q

Liver Functions

A
  • Makes bile
  • Cleans toxins out of blood
  • Removes old blood cells
  • Stores glycogen/vitamins
  • Converts glycogen (starch) to sugar
  • Breaks down fatty acids
99
Q

Bile

A
  • Stored in gallbladder
  • Not an enzyme; it is an emulsifier
  • Involved in physical digestion
  • Contains bile salts which aid in fat digestion
  • When fats are in stomach, signal hormone CCK → blood → gallbladder → trigger gallbladder to release bile salts
100
Q

Small intestine secretions

A
  • Lining of duodenum can also secrete digestive enzymes
  • Peristalsis moves mixture of chyme and digestive juices through intestine
  • Most digestion complted in duodenum
101
Q

At the end of digestion

A
  • Carbohydrates hydrolyzed to monosaccharides
  • Proteins break down into individual amino acids
  • Fats hydrolyzed by lipase into glycerol and fatty acids
102
Q

Small intestine secretions

A
  • DNA will also be digested in the enzymes via nucleases
  • Will result in nucleotides that cells use to replicate their own DNA
103
Q

Absorption in the small intestine

A
  • Jejenum and ileum main absorption of nutrients and water into circulatory and lymphatic system
  • Large folds in lining have fingerlike projections called villi
  • Each villi has microvilli
  • Increases absorption even more
104
Q

How do the circulatory, lymphatic, and digestive system interact

A

Each villus has a small lymph vessel and a network of capillaries

105
Q

Lacteal

A

Absorbs fatty acids and glycerol

106
Q

Capillary

A

Absorbs nucleotides, amino acids, monosaccharides

107
Q

Epithelial cells are connected by ____ ____

A

Tight junctions

  • Creates impermeable barrier between the body tissues and digestive juices in the lumen
108
Q

Villi Functions

A

MR SLIM

  • Microvilli (increases SA:V)
  • Rich capillary network (transports digested products)
  • Single-layer epithelium (minimises diffusion distance)
  • Lacteals (absorbs lipids into the lymphatic system)
  • Intestinal glands (exocrine pits release enzymes)
  • Membrane proteins (facilitates transport of products)
109
Q

Methods of membrane transport

A
  • Co-transport (active)
    For: Glucose, Amino Acids
  • Facilitated Diffusion
    For: Monosaccharides
  • Osmosis
    For: Water
  • Simple Diffusion
    For: Triglycerides
109
Q
A
110
Q

Protein Digestion/Absorption

Secondary Active Transport

A

Glucose and amino acids are co-transported with sodium ions

111
Q

Protein Digestion/Absorption

Facilitated Diffusion

A

Monosaccharides, vitamins and minerals are transported by channel proteins

112
Q

Protein Digestion/Absorption

Simple Diffusions

A

Hydrophobic and lipophilic substances (fats) may freely cross the membrane

113
Q

Protein Digestion/Absorption

Bulk Transport

A
  • Vesicles form around fluid containing dissolved materials
  • Pinocytosis takes less time than shuttling materials via membrane proteins
114
Q

Lipid Digestion/Absorption

A

Lipids are insoluble in water and need to be complexed with proteins in order ot be transported in the blood

  • Lipid globules are emulsified by bile salts before being chemically digested by pancreatic lipases
  • Components are combined with protein to form chylomicrons which are transported to the liver
  • Liver converts chylomicrons into soluble lipoproteins
115
Q

Carbohydrate Digestion/Absorption

A
  • Starch is main polysaccharide in human diets
  • Starch is digested via amylase into smaller subunits
  • Glucose monomers are used for cell respiration or processed and stored in the liver as glycogen via glycogenesis (liver)
116
Q

Protein Digestion/Absorption

Protease

A
  • Proteases are secreted in an inactive form so they don’t synthesize the cells that digest them
  • Activated by specific enzymes or chemical agents (low pH)
117
Q

Large Intestine Function

A
  • Absorb water (mineral and salts)
  • Decompose leftover organic material with help of bacteria
  • Produce vitamin K and B and folic acid required for red blood cell production
  • Stores, eliminates solid waste
118
Q

Large Intestine

Bowel Movement

A
  • Buildup signal CNS which promts movement
  • Stinky because of bacteria
  • Removes toxic wastes from body
  • Not enough cellulose (fibre) = less movement
119
Q

Large Intestine

A
  • At the end of the small intestine, undigested material pass through the ileocecal sphincter into larger intestine
  • Large intestine is wide and short

Three sections:

  • Ascending
  • Transverse
  • Descending

Biology 20 IB (10 decks)

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