Haemoglobin, Haemostasis & its Drugs Flashcards
The harm prosthetic group does three things:
- O2 transport
- Electron transport (Fe2+Fe3+)
- Redox rxn enzymes H2O2–>H20
Give me an example of a tetrapyrolle:
Porphyrin
Can Fe2+ transport O2 instead of Fe3+?
Yes dummy. It has to be Fe2+!
Fe3+’s colour looks like
Rust/Brown
What Hb is scarlet red?
Hb02
Hb itself is Blue (T/F?)
False: it’s dark red
HbCN’s colour
Blue
T/F? Hb’s affinity for CO is 300x than that of O2
False. Only 200x.
Old meat and dried blood looks dark brown. Why?
Because Fe2+ lost an electron, got oxidized and is now Fe3+ which is brown looking
Is there any carbon monoxide in your blood RIGHT NOW?!
Yep. 1%.
T/F? Kendrew and Perutz solved the structure of haemoglobin first, then myoglobin.
False. Myoglobin was the first.
Where is myoglobin found?
Storage for use in Muscle.
How are myoglobin and haemoglobin genes related?
Evolved from a common ancestor.
Haemoglobin is monomeric?
Nope. Tetrameric. You’re thinking of Myoglobin eh?
I take out Fe2+ and replace it with Mg2+, what organism am I and what do I with my shiny Mg2+?
Plants. Photosynthesis.
Why are Mb and Hb water soluble?
So proteins won’t precipitate in high concentration in your cells and ruin your whole day.
What is Myoglobin made out of?
75% a-helices secondary structure
a-helices are what handed? how many and how are they designated?
8 right handed from A-H
what is the percentage of deoxyhemoglobin in the blood?
15%
What’s so special about Foetal Hb?
HbF has gamma chains which are higher affinity for O2.
The Hb Gamma chain is a variant of which Hb subunit?
The Adult Hb Beta subunit.
What does Histidine F8 do?
anchors Haem group
What does Histidine E7 do?
excludes H20 from Fe2+ and lets O2 to bind
T/F? Oxygen pulls the iron atom out of the plane of the Haem
False.
When O2 binds, Histidine F8 is pulled too and what happens?
changes the tertiary structure of the whole damn subunit.
After one subunit changes then what?
The other three follow suite like lemmings. Cooperative change.
In oxyheme the H-bond is where?
between His E7 and one of the oxygens
in deoxyheme where is the H-bond?
between alpha and beta subunits
Explain the T-form of haem:
T=tense due to 8 salt bonds in deoxy-Hb
R form of Hb: explain!
R=relaxed, oxyhaemoglobin and is a relatively open structure
What is the deoxy state locked by?
Asp-Tyr H-bond
What is the oxystate locked by?
Asn-Asp H-bond
What the heck is BPG?
2,3-bisphosphoglycerate is n allosteric effector of Hb.
Hb at P50 is?
26 torr
1 atm is how many Torr?
758 mmHg
758 mmHg is how many kPa?
101
what is P50?
pressure of half saturation
What animal has an uncomfortable amount of myoglobin?
Whales.
What’s the second meaning of Allosteric?
A protein with sigmoid kinetics
Acid shift the curve to the?
Right
Alkalosis shifts the curve to the?
Left
How do you explain the sigmoid shape of Hb?
Due to cooperative binding/unbinding of O2 via the subunits.
What’s the Bohr effect?
acid stims HbO2 to yield more O2 via stabilizing the heme
Altitude adaptation shifts the curve to the?
Right.
How does Altitude adaptation work?
elevation of 2,3 BPG from 4.5mM to 7mM
How are red cell numbers increased?
kidneys release EPO
Foetal haemoglobin’s saturation curve shift which way?
Left