03 - Lecture 19 Flashcards
(15 cards)
What is the pH of pepsin and function?
pH of 2, pepsin is a digestive enzyme
How is trypsin formed?
Trypsin is formed by proteolytic cleavage
Km and affinity relationship?
HIGH affinity = LOW km
How do you increase Vmax?
You increase Vmax by increasing the amount of enzyme
Competitive inhibition?
- No enzyme substrate complex but a enzyme inhibitor complex
- Need more substrate which produces the apparent Km
- Most drugs are competitive inhibitors
Noncompetitive inhibition?
- Different binding site for inhibitor
- Different Vmax (apparant Vmax)
- Same Km – no competition
Irreversible inhibitor
Will bind to an enzyme so no other enzyme-substrate complex can form.
- DFP (nerve gas), acetylcholinesterase doesn’t breakdown the acetylcholine so the Na channel stays open which results in uncontrolled firing of nerve impulses = seizure
If you want to activate coagulation and protect the stomach from acids what does the trick?
COX-1
What does aspirin do?
Aspirin is an irreversible inhibitor of COX 1 and 2.
- blocks the signaling for coagulation (COX-1) by binding to COX-1
BAD - can lead to gastric ulcers and bleeding from stoping the production of prostaglandins
Does Aspirin unbind from COX-1 enzyme?
No you have to wait for your body to produce new platlet cells with new COX-1
What causes fever, inflammation and pain ?
Prostaglandins
What is a low dose of aspirin for?
To stop blood clotting in a patients that have a likelihood of blood clots, stroke, heart attack
- 81 mg
What do you always need to have in the blood?
Thromboxane and Prostacyclin
Suicide inhibitor drugs
Bind to the active site of enzymes. For example penicillin binds to the active site of the enzyme that forms bacterial cell walls = resulting in the bacteria not having a cell wall
How to treat gout?
Allopurinol - no uric acid is produced
