Lecture #13 - Biotech 1 Flashcards
Therapeutic proteins - non-human sources:
What problem? (2)
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Therapeutic proteins - human sources:
What problems could this cause? (3)
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Therapeutic proteins - recombinant human proteins:
What does this allow?
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Recombinant insulin - how is it done?
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List 3 advantages and 2 disadvantages of using prokaryotic systems
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Erythropoitein (EPO):
- When was this gene cloned?
- What kind of PTM does this go through?
- What is this PTM important for?
- What is this protein made in?
- How many aa’ is this protein and is that big/small?
- How many and what kind of secondary structure?
- What kind of protein is it (enzyme, transporter etc)
- Produced mainly by what?
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Expression vector for EPO - what does it look like?
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EPO regulated haematopoeiesis:
- Its synthesis and release is regulated (in part) by what? What does this mean if you are in a low oxygen environment?
- Epo stimulates what two things?
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What two things can affect EPO levels (leading to what?)
How can you restore red blood cell levels?
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Why is EPO used as a performance enhancing drug? (3)
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Detecting EPO - how? What’s the problem with that nowadays?
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Recombinant antibodies:
- Why are they increasingly being used?
- Most therapeutic AB target what?
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Making an AB to TNF-alpha:
- Why target this? (2)
- What was developed to bind and neutralise TNF-alpha?
- What is a monoclonal AB?
- How do you make a mAB?
- What problems could this cause?
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Infliximab:
What is it?
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Since cells can’t perform all PTM equally well (e.g. gla which is needed for blood clotting processes), what do they do now? What example did she use?
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