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biopharm > module 6 > Flashcards

module 6 Flashcards

1
Q

what are biologic drugs

A
  • vaccine, protein, antibody, nucleic acid
  • high molecular weight
  • manufactured using living things
  • generally injectable
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2
Q

describe diabetes

A
  • family of metabolic disorder
  • characterized by high blood sugar
  • cardiovascular, kidney, skin ulcer, eye damage
  • top 10 disease in Canada
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3
Q

how are blood glucose concentrations regulated

A
  • using insulin, hormone produced by pancreas
  • regulates metabolism of carbs, fats, and proteins
  • promotes absorption of blood glucose by fat and liver cells convert glucose into glycogen or fat
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4
Q

function of insulin

A
  • regulates metabolism of carbs, fats, and proteins
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5
Q

what do high and low insulin levels mean

A
  • high means low blood sugar (glucose to glycogen)
  • low means high blood sugar (glycogen to glucose + protein catabolism)
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6
Q

describe type 1 diabetes

A
  • 10% of population
  • starts in childhood
  • autoimmune component
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7
Q

describe type w diabetes

A
  • 90% of population
  • insulin resitance
  • pancreas produces insulin but cells do not respond
  • autoimmune component
  • obesity
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8
Q

when was insulin first marketed

A
  • 1922-1923
  • failed because impurities and not enough amount
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9
Q

first experiment with insulin

A
  • surgically altered dogs to enable insulin isolation
  • pancreatic ducts tied off causing cell death
  • leaving behind islets of langerhans
  • isolated insulin extract from islets
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10
Q

sources of commercial animal derived insulin

A
  • pancreas harvested
  • bovine: cows
  • porcine: pig
  • equine: horse
  • ichthyic: fish
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11
Q

what were the issues with animal sources

A
  • proinsulin(allergenic): overtime patients could become allergic, require diff animal source
  • glucagon
  • somatostatin
  • proteases: slowly destroy other proteins in drug, limit shelf life
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12
Q

what were general insulin isolation methods in 1920s

A
  • truck load of pancreases
  • homogenization
  • clarification (2)
  • serial precipitation (2)
  • chromatography (3)
  • recrystallization

T H C S I P I S R

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13
Q

describe homogenization

A
  • break open organ/cells containing protein to be extracted
  • blender, sanitation, osmotic shock
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14
Q

describe clarification

A
  • separate liquid fraction of biological isolate from solid fraction
  • 2 methods: dialysis and centrifugation
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15
Q

describe clarification: dialysis

A
  • use continuous diffusion through semi permeable membrane
  • placed between mixture and buffer
  • membrane allows solutes to pass through while keeping solids behind
  • solutes pass from high concentration (mixture) to low concentration
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16
Q

describe clarification: centrifugation

A
  • centripetal force creates artificial gravity
  • causes solids in suspension to sink quickly to bottom where they form pellets
  • liquid decanted from solid
17
Q

describe serial precipitation

A
  • to isolate compounds
18
Q

describe serial precipitation: isoelectric precipitation

A
  • causes certain proteins to precipitate from solution, other proteins left behind, BY CHANGING IONIZATION
  • changes pH of solution which alters the charge state of proteins depending on amino acid side chain patterns
  • if net number of charges is equal then protein is at isoelectric point
  • isoelectric point: neutral and insoluble in water, precipitates leaving other substances behind
19
Q

describe serial precipitation: denaturing precipitation

A

Causes certain proteins to precipitate from solution, other proteins left behind, BY CHANGING CONFORMATION

  • pH, solvent polarity (add non polar or salts), heat
  • done in several ways, conditions made to cause proteins to change conformation (denature) which changes solubility and leads to precipitation
  • changed pH of solution alters the charge state of proteins depending on amino acid side chains, change in ionization changes non bonding interactions that maintain conformation
  • adding alcohols or other non polar solvents directs VDW in the centre, may expose electrostatic interactions or h bonds in centre to water which can weaken these interactions causing protein to change shape
  • heating solution can increase moeclulue motion, if protein flexes enough to allow water to penetrate into NP portions, can disrupt electrostatic interactions or h bonds in centre, weaken these interactions causing protein to change shape
20
Q

describe chromatography: ion exchange

A
  • pass mixture in solution through ion exchange column using buffer at specific pH
  • pH sets ionization state of each protein in mix
  • solid phase on column is covered in ionized groups (+/-) attract opp charged proteins
  • neutral molecules or molecules w same charge not attracted and pass quickly through column
  • molecules with opposite charges pass slowly.
  • speed determined by overall charge
  • anionic resin for cationic exchange
21
Q

describe chromatography: size exclusion

A
  • molecules separated according to size
  • pass mixture through size exclusion gel
  • gel contrans pores of a set size
  • small molecules fit and stuck
  • pass through gel slowly
  • large not fit and go quickly
  • intermediate partly and speed depending on how much they get stuck
22
Q

describe recrystallization

A
  • dissolve mixture in minimum hot solvent
  • solvent should dissolve impurties
  • solvent show dissolve desire molecules well at high temp and poor at low
  • after dissolving, solution cools, crystals of desired molecule precipitate from solution
  • impurities remain in solution
  • works well if desired is bulk not minor component
23
Q

what is HPLC

A

High Pressure Liquid Chromatography

24
Q

what are challenges ti drug manufacturing using animal sources

A
  • proteins not human
  • purity
  • large amounts
25
Q

describe the general structure of insulin

A
  • small oriteubm 2 chains
  • A: 21 amino acids, intrachain disulphide bond
  • B: 30 amino acids
  • connected by 2 disufide bonds
26
Q

similarities between human and animal sequences

A
  • A chains the same
  • Porcine is 1 amino acid different in B chain
27
Q

what are the limitations to chemical synthesis

A
  • small quantities
  • large waye
  • only 20 amino acid chain length
28
Q

what are the goals of protein drug manufacture

A
  • high purity
  • large amounts
  • human
  • low cost and waste
29
Q

what was the first synthetic gene

A
  • somatostatin (expressed in coli)
30
Q

first genetically modified drug

A

recombinant insulin

31
Q

first recombinant drug

A
  • humulin (thought to be safe but rather better supply)

biopharm (8 decks)

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