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44 Cards in this Set

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Protein C
Anti-coagulation protein
Activated form is Protein Ca.
Activates fibrinylosis
What is Warfarin? It works by...
Anti-coagulation medicine.
Inhibiting Vitamin K epoxide reductase -- the Reduction of Vitamin K (so that it can be used again in coagulation).
Warfarin blocks...
regeneration of Vitamin K and blocks coagulation.
Warfarin has shown to have variable effects among patients because....
Of the variation in the genes for Cytochrome and Complex 1 of the Vitamin K epoxide reductase.
Name the two pathways for coagulation...
Intrinsic (Kininogen)
Extrinsic (trauma - tissue factor)
Which factor is common between intrinsic and extrinsic coagulation pathway?
Factor X and Xa (and everything following that....Thrombin, Fibrinogen, XIIIa)
Which factor is common to coagulation and anticoagulation pathways?
Thrombin
Name 4 things that impact k (rate of a reaction)?
pH
Ion concentration
Temp
Activation energy (can be lowered with a catalyst)
V (reaction rate) =
k[a][b] (A and B are substrates)
What is a first order and a second order reaction?
First order - One reactant

Second Order - two reactants
Rate of a reaction increases when...

As the substrate is consumed, the rate of reaction....
The concentraion of substrate increases.

Decreases.
What is Michaelis constant?
It is only associated with rate constants.

Km is substrate concentration at which the velocity is half the maximum velocity.

Km = (K-1 + K2)/K1
When can a rxn be at Vmax?
When the enzyme is saturated. (All of the enzyme is being used so the rate can not increase anymore, even if more substrate is available).
What is dissociation constant
[E][S]/[ES]
What is "a measure of enzyme concentration for significant catalysis to occur"?
Turnover number.
What is "a meaasure of substrate concentration when half of Vmax is reached"?
Km
Define "enzymes"
Biological chemicals that increase rate of chemial reactions.
Catabolism

Anabolism
Catabolism - Energy production. Fuel oxidation.

Anabolism - Energy consumption. Reduction process.
What is apoenzyme?

Wheat is haloenzyme?
An enzyme without its cofactor is called apoenzyme.

An enzyme with a cofactor is called haloenzyme.
Vitamin E deficiency
Inhibition of sperm production
Vitamin K deficiency results in....
Subdermal hemorrhaging (this vitamin helps with blood coagulation)
What are the cleavate sites for following proteases?

Chymotrypsin
Trypsin
Thrombin
Proteinase K
Chymotrypsin - Aromatic residues on the carboxyl side of the bonds
Trypsin - Carboxyl side of Arg and Lys
Thrombin - Between Arg and Gly
Proteinase K - Lacks residue specificity.
Describe the two models of enzyme-substrate complex?
Lock and Key - Enzyme structure remains the same.

Induced Fit - Dynamic recognition. Enzyme changes its shape as the substrate binds to it.
What is a catylytic triad?
Three potentially charged residues near one another in the interior of the enzyme.

Serine, Histidine and Aspergine.
What is the function of transglutamidase?
Transglutamidase (Factor XIII) stabilizes soft clot between fibrin monomers and creates hard clot.
What is "Proteinase Active Receptor"?
Activated thrombin receptor.
What is "von Willerband's factor"?
It is a glycoprotein that helps platlets bind to activated thrombin receptor.
What is the importance of gama-carboxyglutamate?

It is produced using....
It binds to phospholipid surface with the help of Ca2+.

This factor is produced using Vitamin K.
Protein C is a....

Activated by...

Describe the cascade...
Major factor in regulation of coagulation.

Activated when Thrombin binds to thrombomodulin (thrombomodulin is on the surface of endothelium)

Protein C >> Protein Ca >> blocks tPA inhibitor >> Active Plasmin increase (which digests fibrin clot)
What is the function of urokinase?
It maintains Active plasmin levels in the plasma.
What is tPA?
tPA activates plasmin (part of fibrinolysis).

tPA inhibitor is blocked by Protein Ca.
What Protein S?
Protein S is derived from Protein Ca.

It is a cofactor that helps in anticoagulation by blocking Va and VIIIa.
How does heparin impact coagulation?
Heparin binds to Antithrombin and causes Xa to bind to antithrombin.

Xa bound to antithrombin is in inactive form and hence, this stops clotting.
What is Km?
Km is a measure of SUBSTRATE concentration required for significant catalysis to occur.
What is turnover number?
Applies when the enzyme is completely saturated by substrate.
What is an isozyme?
An enzyme that catalyes the same chemical reaction (this enzyme comes from different genes and has different amino acid sequence).
Give two examples of enzymes that have isoforms.
LDH (heart and myocyte)
Creatinine Kinase
What is negative cooperativity?
Negative cooperativity - When binding of the substrate to an enzyme decreases enzyme activity.
Prothrombin is activated by...
Va, Xa and Phospholipids
Factor X is activated by...

Intrinsic pathway

Extrinsic pathway
Intrinsic - IXa, VIIIa

Extrinsic - VIIa and TF
Soft clot is stabilized by...
Transglutamidase....covalent bonds.
Transglutamidase is responsible for
stabilizing the soft clot and forming hard fibrin clot (factor XIIIa)
Why does glutamate acid need to be carboxylated during coagulation?

What assists in this carboxylation?
Negatively charged carboxylated groups bind to the membrane phospholipids. (Membrane is also negatively charged, so Ca+2 is required for this interaction).

Vitamin K is vital in the carboxylation of Glutamate acid.
How does Warfarin work?
Anticoagulation medication

Warfarin blocks reduction of Vitamin K epoxide. This inhibits formation of gama-glutamidase and blood clotting.