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Chemistry > Unit 3 > Flashcards

Unit 3 Flashcards

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1
Q

hazard control

A
  1. engineering controls (changing work environment ie. fume hood)
  2. administrative controls (protocols)
  3. procedural controls (modify work behaviour ie. substituting for less hazardous)
  4. PPE
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2
Q

SDS

A
  1. chemical and company info
  2. composition
  3. hazards
  4. first aid
  5. fire fighting
  6. accidental release
  7. handling and storage
  8. exposure controls/PPE
  9. physical and chemical properties
  10. stability + reactivity
  11. toxicology
  12. ecology
  13. disposal
  14. transport
  15. regulations
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3
Q

workplace label

A

required when transferred to another container, but not if the product is being used immediately

  • includes name, safe handling precautions, SDS reference
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4
Q

standard operating procedures (SOPs)

A

describe material and methods and precautions
- think through the procedure step by step and standardize
- must be clear, concise, follow the sequence of operations activities

  • instructions, PPE required, materials/equipment required, sample/material limitations, disposal

can be for: equipment, chemicals, inventory, disposal, archiving

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5
Q

units

A

kilo (K) = 1000
deci (d) = .1
centi (c) = .01
milli (m) = .001
micro (weird symbol) = .000001 (5 0s)
nano (n) = .000000001 (8 0s)

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6
Q

%

A

concentration of solute in a solvent

w/v = weight of solute/volume of solvent

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7
Q

molarity

A

of M of solute/1 L solvent

(1 M = mass of molecular weight in grams)
- add atomic weights of atoms together

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8
Q

osmolality

A

measurement of solute concentration in fluid
- high osmolality = high solute concentration

if osmolality of blood increases it triggers desire to drink + release of antidiuretic hormone

if osmolality of blood decreases it inhibits desire to drink + inhibits release of antidiuretic hormone

serum osmolality tests assess: hydration, hyperglycemia, hypothalamus function, ethylene glycol poisoning

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9
Q

antifreeze poisoning

A

ethylene glycol causes reaction in liver and kidneys as they try to metabolize -> converts into toxic metabolites

causes metabolic acidosis and nephrotoxosis (eg. oxalate is cytotoxic)

treatment:
- IV therapy (often incl. sodium bicarbonate to counteract excessive acid) to restore hydration, electrolyte balance, kidney function, and excretion of ethylene glycol
- solution of diluted ethanol (competes with ethylene glycol for binding site on enzyme)

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10
Q

isotonic fluids

A

osmolality mimics normal blood
- extracellular and intracellular fluids have the same concentration of dissolved substances

eg. 0.9% NaCl (normal saline)

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11
Q

hypotonic fluids

A

osmolality less than blood
- more solutes in intracellular (cytoplasm) than in extracellular fluid
- makes water flow into cell -> swell -> burst

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12
Q

hypertonic fluids

A

osmolality greater than blood
- higher solutes in extracellular fluid than intracellular (cytoplasm)
- water leaves cell -> shrinks + shrivels

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13
Q

electrolytes

A

most abundant solute in body

  • most able to cause fluid shifts between compartments
  • concentration expressed as milliequivalents/L
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14
Q

organic molecules

A

large solute, not as numerous

  • uneven distribution b/w fluid compartments
  • eg. proteins, phospholipids, cholesterol, triglycerides
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15
Q

water movement

A

occurs from change in concentration of any solute
- water moves from one compartment to another

  • crosses cell membrane OR crosses capillary walls
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16
Q

edema

A

accumulation of excess fluid in tissue
- indicates abnormal movement of fluid from vascular pace into interstitial space

eg. pulmonary edema, cutaneous edema

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17
Q

types of fluid

A
  1. crystalloid
    - lots of electrolytes (hypo or isotonic)
    - small solutes -> cross vascular wall
    - rehydrate extravascular spaces
    - correct acid/base imbalance
  2. colloid
    - heavy molecules suspended in isotonic crystalloid
    - solutes too large to cross vascular wall
    - ‘hold’ fluid in intravascular spaces
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18
Q

membrane processes

A
  1. absorption of nutrients/excretion of waste through plasma membrane
    - occurs with or without expending energy (ATP)
    - passive process/active process
  2. membrane permeability
    - freely permeable
    - selectively permeable
    - impermeable
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19
Q

diffusion

A

kinetic movement of molecules from high -> low concentration

factors:
- molecular size
- lipid solubility
- molecular charge (channels let certain ions through)

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20
Q

facilitated diffusion

A

selective ‘carrier proteins’ assist in moving molecule from high -> low concentration

  • # of carrier proteins available limits the process
  • no ATP required
  • eg. glucose moves into muscle and fat cells
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21
Q

osmosis

A

passive movement of water through semipermeable membrane

  • low -> high concentration
  • osmotic pressure: force of water moving from one side of membrane to the other from difference in solute concentration
  • concentration balance = equilibrium
  • eg. water moves from stomach into bloodstream
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22
Q

oncotic pressure

A
  • there is a difference between osmotic pressure of blood + osmotic pressure of interstitial fluid/lymph
  • maintains fluid balance
  • imbalance if protein levels in plasma decrease (eg. subcutaneous edema, ascites)
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23
Q

filtration

A

based on pressure gradient
- liquids pushed through membrane if more pressure on one side

  • eg. hydrostatic pressure (caused by heart beating), filters blood in kidneys
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24
Q

dialysis

A

type of diffusion used clinically in animals with kidney failure

  • to remove toxins from blood, it is circulated through artificial kidney with semipermeable filaments
  • electrolyte solution (dialysate) driven through fake kidney in opposite direction of blood -> small solutes move out of blood into the lower concentrated electrolyte solution
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25
Q

active membrane processes

A

movement across cell membrane requiring ATP

molecules can’t enter passively because:
- not lipid soluble
- too large
- going against concentration gradient

  1. active transport
    - symport
    - antiport
  2. cytosis
    - endocytosis
    - exocytosis
26
Q

active transport

A

carrier protein + ATP required to move:
- Na, K, Ca2, Mg2

a. symport
- substances moved in same direction

b. antiport
- some substances in same direction, some in opposite

27
Q

ionic concentration

A
  • critical for maintaining fluid balance
  • critical for normal functioning of irritable cells (those which create energy for active transport through respiration)

ie. myofibrils, neurons

28
Q

cytosis

A

brings nutrients into cell + ejects waste
- needs ATP

a. endocytosis
- transports large particles/liquids into cell by engulfing them
- phago, pino, or receptor-mediated

i. phagocytosis: cell eats solid material by making a vesicle (‘phagosome’)
- marcophage: debris, dead cells, invaders
- phagosome fuses with lysosomes for digestion
- white blood cells handle bacteria and viruses
- pseudopodia: macrophages + WBC move by amoeboid motion

ii. pinocytosis: cells engulfs liquid material through infolding of plasma membrane
- in cells lining small intestine and renal tubules

iii. receptor-mediated endocytosis: for cells with specific proteins in their plasma membranes
- eg. ‘ligands’ bind to specific receptors making a vesicle known as ‘coated pit’
- eg. insulin binding to insulin receptors

b. exocytosis
- export intracellular substances into extracellular space
- substances packaged in vesicles by ER + golgi body
- vesicles move through cytoplasm -> cell surface -> fuse w/plasma membrane -> release contents into extracellular fluid
- eg. neurons release acetylcholine
- eg. endothelial cells lining trachea secrete mucus
- eg. mast cells release thousands of granules of histamine during alleric reaction
- excretion = waste
- secretion = manufactured

29
Q

membrane potential

A

AKA voltage
- potential electrical energy created by separation of opposite charges (changes in distribution of charged particles on either side of cell membrane)
- plasma membrane more permeable to some molecules than others
- ALL cells have membrane potential (normal values -20 to -22 millivolts/mV)

  • principal ions: K and Na
  • normally more K inside a cell, moves out by diffusion
  • Na more outside cell, can’t easily move in, occurs at every cycle of active transport
  • 3 Na exit for every 2 K entering
  • ‘resting membrane potential’ altered by:
  • changes in environmental tonicity, osmotic pressure, temperature, or contact with neighboring cells
  • these changes alter flow of metabolites (alters behaviour of structural and enzymatic proteins)
  • eg. muscle cells contracting due to changes in membrane potential
30
Q

6 main nutrients

A

nutrient: substance from food used to carry out body functions

  1. water
  2. carbohydrates
  3. lipids
  4. proteins
  5. vitamins
  6. minerals
31
Q

3 energy producing nutrients

A

carbohydrates
lipids
proteins

32
Q

3 non-energy producing nutrients

A

water
vitamins
minerals

33
Q

essential nutrients

A

body can’t manufacture, must get from diet

eg. taurine in meat, cats need to prevent retinal degeneration, dilated cardiomyopathy, decreased reproductive function

34
Q

water

A

most important nutrient
- amount needed = daily energy requirement
- from food, drink, oxidizing proteins/fats/carbs

35
Q

nutrient groups + dietary sources

A

p. 418-428

36
Q

glucose

A

monosaccharide
- simplest dietary carb
- makes ATP through glycolysis
- excess converted to glycogen -> stored in liver OR converted to fat + stored in adipose

37
Q

fatty acids

A

saturated:
- single bonds b/w C, can accommodate greatest # of H
- long chains

eg. meat and dairy

unsaturated:
- 1+ double C bonds, less room for H
- liquid at room temp
- monounsaturated: olive, peanut oil
- polyunsaturated: corn, soybean, safflower oil

  • liver can convert one fatty acid into another

essential: can’t be synthesized
- linoleic
- linolenic
- arachidonic acid

38
Q

neutral fats

A

2x as much potential energy as proteins or carbs.
- make food taste good
- stave off hunger
- help absorb fat-soluble vitamins: A D E K
- insulate when stored, protect and cushion vital organs

  • rebuilt by liver -> form different kinds of triglycerides
  • major energy source for hepatocytes and skeletal muscle cells
39
Q

protein all or none rule

A

for body to make a new protein, all of the needed amino acids (essential + non) must be present in the cell
- in sufficient quantity
- present at same time

if one is missing, the protein can’t be made

40
Q

essential amino acids

A

can’t be made at all or fast enough for body’s tissue maintenance

eg. taurine, arginine, glycine

41
Q

proteins

A

complete/’ideal’:
- all essential amino acids needed by species to meet its metabolic requirements (meat, eggs, dairy)

complements:
- when ingested together, contain all amino acids (legumes and grains)

biologic value:
- % of absorbable protein available for body functions (not same as protein content)
- quality of protein improves when feed is not overprocessed/overheated

ruminant digestion of protein:
- facilitated by microbes
- microbial-made protein has consistent quality regardless of source (lower-quality feed is improved by microbial metabolism)
- ability to convert non-protein sources of N into protein

42
Q

nitrogen balance - amino acids

A

amino acids can’t be stored. if not used to make protein immediately then:
- oxidized by cell for energy
- converted to carbs or fats

  • rate of protein synthesis = rate of protein breakdown/loss
  • positive balance: more protein incorporated into tissue than is used to make ATP (healing, pregnancy, growth)
  • negative balance: protein breakdown exceeds amount incorporated into tissue (stress, infection, poor dietary protein)
  • N from protein breakdown packaged into ‘urea’ in liver -> excreted by kidney
  • urea measured by blood urea nitrogen (BUN) test
43
Q

vitamins

A

essential for life
- don’t make energy
- not broken into building-block units

not made in body EXCEPT:
- D (made in skin)
- K + biotin (made by bacteria in intestine)
- A (made by converting beta carotene)

function:
- co-enzymes/parts of co-enzymes
- molecular structure is the ‘key’ to activate an enzyme
eg. riboflavin + niacin breakdown glucose

water-soluble vitamins:
- absorbed through GI wall
- very few stored (hypervitaminosis would be rare), excess excreted in urine
ex. C, B (except B12)

fat-soluble vitamins:
- bind to ingested lipids before they’re absorbed with food
- stored in body (except K), hypervitaminosis can occur
ex. A, D, E, K

44
Q

free radicals

A

generated when carbs, proteins, and fats are oxidized as part of normal metabolism
- potentially harmful
- disarmed by antioxidants (vitamins A, C, E)

45
Q

minerals

A

inorganic substances essential for life
- non-energy
- work with other nutrients for body function

3 classes:
1. macro
2. micro
3. trace elements

46
Q

chemical reactions

A

forming and breaking chemical bonds

4 types:
1. redox
2. synthesis
3. decomposition
4. exchange

factors influencing:
1. concentration of reactants
2. temperature of environment
3. activation energy
4. catalyst presence

47
Q

redox reactions

A

an e- removed during oxidation of atom/molecule is transferred to another atom/molecule -> the one that gains an e- is ‘reduced’ -> the one that loses an e- is ‘oxidized’

a) oxidation
- combine with O, lose H and e-

b) reduction
- combine with H, gain e-, lose O

48
Q

synthesis

A

smaller molecules bond to form larger complex molecules
- anabolic process in body

eg. amino acids join to form a protein molecule

49
Q

decomposition

A

bonds in large molecules broken to make smaller less complex molecules
- catabolic process

eg. glycogen breaking down into glucose

50
Q

exchange

A

bonds broken + made

eg. ATP transfers 1 phosphate to glucose -> ‘glucose-phosphate’

51
Q

catabolism

A

cell metabolism where nutrients broken down to make energy
- energy stored in bonds of ATP molecule -> transported where needed

stages:
1. GI tract
- broken down in stomach -> small intestine -> nutrients absorbed by cells that line small intestine -> nutrients pass to blood/lymph -> carried to organs + tissues -> may go to liver for further metabolism
- enzymes help
- hydrolysis into building blocks:
- carbs break down -> monosaccharides
- fats break down -> fatty acids + glycerol
- proteins break down -> amino acids

  1. cytosol
    - anaerobic respiration in cell cytosol catabolizes nutrients
    - acetyl CoA transported through cytoplasm to mitochondria.
  2. mitochondria
    - aerobic respiration in cell mitochondria (happens by PO4 attaching to ADP -> ATP)
    - ATP used to help cell carry energy
    - catabolic pathways of proteins, carbs, and fats transfer energy stored in nutrients into ATP
52
Q

anabolism

A

cell metabolism where stored energy makes new molecules from small components that catabolism made

  • biosynthetic process
  • growing cells need additional proteins for the expanded cell membranes and to perform vital functions

metabolic turnover:
- replacement molecules must be manufactured continuously

dehydration synthesis:
- part of anabolism
- opposite of hydrolysis
- monosaccharides assembled into polysaccharide chains
(1 mono + 1 mono = 1 di + water)
- fatty acids + glycerol assemble fat molecules
- amino acid chains assemble proteins

53
Q

energy for metabolic reactions

A
  • energy supplied to cells by nutrient breakdown
  • energy released when bonds broken

storage forms: ATP, NADH, FADH2

54
Q

control of metabolic reactions

A
  • metabolism is a multi-enzyme sequence of events
  • reactions are highly specific, enzymes initiate and control metabolism
  • each enzyme reacts with ONE particular molecule (substrate) to produce new molecule (product)
  • product of one step = substrate of next
  • cofactor:
  • nonprotein that might be needed to help complete a reaction
  • completes the shape of a binding site
    eg. iron, zinc, copper, magnesium, potassium, calcium ions
  • co-enzymes:
  • nonprotein organic molecules that can be co-factors
  • often vitamins/vitamin-derived
  • can be temporary/permanently bound to enzyme
    eg. NAD, acetyl-coenzyme A, FAD
55
Q

enzyme activity

A

depends on molecular shape of enzyme
- enzymes remain unaltered from reactions.
- end in ‘-ase’, often named for the substrate the act upon
eg. phosphotransferase moves PO4 group

active site = region where it binds to substrate

factors affecting enzyme activity:
- enzyme concentration (effect on rate directly proportional)
- substrate concentration (rate increases until enzyme is saturated)
- temperature (rate increases until denaturation of enzyme)
- pH (most max out at pH 7 and denature at pH extremities except pepsin [1.5 optimum])

eg. shape of binding site in some enzymes affected by temperature (‘thermolabile enzymes’), such as siamese coat color enzyme which doesn’t function well in heat so only its extremities get the dark coloring

56
Q

catalytic efficiency

A
  • enzymes act as catalyst
  • speed up reactions by lowering activation energy
  • this increased rate is essential to life
    eg. Co2 (waste from respiration) needs to be moved out of body -> carbonic anhydrase combines with CO2 -> ‘carbonic acid’ + bicarbonate ions
57
Q

enzyme inhibition

A

inhibitor: any substance that can decrease rate of enzyme-catalyzed reaction
- many poisons, some medicines
- some inhibitors provide internal regulation of cellular metabolism

2 kinds:
1. reversible
- binds to an enzyme but can be removed
a) competitive
- competes w/substrate for binding at active site of enzyme
- similar molecular structure to the normal substrate
- reversed by increasing concentration of normal substrate
- competition won by whichever is in greater concentration
eg. sulfa drugs
eg. folic acid needed by bacteria is synthesized from p-aminobenzoic acid, which resembles sulfanilamide -> sulfanilamide competes for active site -> synthesis of folic acid slowed/stopped -> bacteria prevented from multiplying

b) noncompetitive
- binds to enzyme at location other than active site
- no resemblance to normal enzyme substrate
- interactions makes shape of enzyme + active site change
- enzyme no longer binds normal substrate or it binds improperly so creation is not catalyzed
- more substrate does NOT reverse inhibition
eg. isoleucine feedback inhibitor

  1. irreversible:
    - covalent bond w/ functional group of enzyme
    - makes enzyme inactive
    eg. many poisons….

eg. cyanide ion:
- interferes w/ cytochrome oxidase
- blocks mitochondrial e- transport chain
- stops aerobic cellular respiration
- death in minutes.
- antidote: sodium thiosulfate (converts cyanide ion to thiocyanate that doesn’t bind cytochrome oxidase)

eg. heavy metals (mercury, lead)
- combine sulfhydryl groups on enzymes
- can cause neurological damage
- treated with chelating agents (substance that combines with metal and holds it tightly)

eg. antibiotics (penicillin)
- inhibit enzymes essential to life processes of bacteria
- interferes w/ transpeptidase which is needed for bacterial cell wall construction

58
Q

regulation of enzyme activity

A

enzymes must be controlled (organism responding to changing conditions and cellular needs)

3 control mechanisms:
1) activation of zymogens
- enzymes may be synthesized as inactive precursors called zymogens or proenzymes
- stored in inactive state
- when needed, zymogen is released and activated at location of reaction
- activation usually involves cleavage of peptide bones of zymogen
eg. active enzyme ‘thrombin’ -> zymogen ‘prothrombin’

2) allosteric regulation
- combination of enzyme with compound (‘modulator’) that changes shape
- modulators may be: activators (increase activity) OR inhibitors (decrease activity)
- allosteric enzymes often located at key control points in cellular processes
eg. synthesis of isoleucine - 5 steps
- product isoleucine binds to enzyme at 1st step -> inhibits enzyme -> no excess isoleucine produced -> when isoleucine level lowers the enzyme will be more active -> more isoleucine synthesized
—> this is an eg. of ‘feedback inhibition’: a process where the end product of a pathway inhibits an earlier step in the process

3) genetic control
- enzyme induction: synthesis of an enzyme in response to cellular need
- allows organism to adapt to environmental changes
eg. regulation of gluconeogenesis (activity of PEP carboxykinase increased during fasting, starvation and diabetes mellitus due to enzyme induction by glucagon)

59
Q

enzymes in clinical diagnosis

A
  • certain enzymes normally found only inside cells -> released into blood/fluid when cells damaged
  • changes in blood serum levels of specific enzymes can be used to clinically detect cell damage or uncontrolled growth
  • measurements of enzyme concentrations is a major diagnostic tool for heart, liver, pancreas, and bone diseases

eg.
- alkaline phosphatase: liver/bone
- amylase: pancreas
- lipase: acute pancreatitis
- alanine transaminase: hepatitis
- aspartate transaminase: hepatitis/heart attack

60
Q

isozymes

A

slightly different form of the same enzyme produced by different tissues.
- similar catalytic properties but different physical properties
- assays for isozymes can pinpoint location and type of disease accurately

Chemistry (5 decks)

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