Blood
aqueous solution that functions as a transport and distriubution system for the body
Serum Vs plasma
Plasma
-aqueous solution obtains following centrifugation of blood treated with anticoagulants
Anticoagulants:
1)EDTA- ethylenediamine tera acidic acid prevents coagulation by chelating divalent cations (Ca2+ and Mg2+)
2)Heparin-prevents coagulatin by binding to thrombin
3) citrate- used when blood is transfused
Serum
Erythrocytes
RBC
transport Due to hemoglobin
-oxygen, CO2, and protons
Cellular remnant
Metal Transport/ Storage Proteins
Albumin
Functions: protein reserve, osmotic regulator, transport protein
Transferrin (fe2+)
-transports ferric iron(fe3+)
Ferritin
-iron storage protein; measured to determine iron def
Enzyme def
a protein or RNA molecule that catalyzes a biochemical rxn
Properties of Enzymes
1) Active site- 3D pocket or cleft created by catalytic groups-R groups of amino acids interact together causing the protein to fold and forming tertiary structure
- speicfic for particular substrate/rxn
2) Enzyme helper molecules
- cofactor
- coenzyme
- prosthetic group
* *prosthetic group and coenzyme derivatives of vitamins
3) Catalytic efficieny
- increase rate of rxn over uncatalyzed rxn
- 100 to 1000 S -> P/sec
- turnover
4) regulation
- enzyme can be activated or inactivated
5) compartmentalization-E are localized in particular compartments within a cell
Enzymes alter Rate but DONT
1) Enzymes do not change equilibrium of reaction
- amount of product is the same despite the prsecen/absene of enzyme
2) Rate is significantly different in enzyme catalyzed and uncatalyzed reactions
3) Enzymes accelerate the attainment of equilibrium but do not shift their position. The equilibrium position is a function of free energy difference between R and P
Enzymes accelerate reactions by lowering activation E (G=) by facilitating the formation of transition state
Evidence of ES
1) Saturation of Active site by increasing [S]
- at constate [E], velocity increases with increasing substrate conc until a maximal velocity is reached
- at maximal velocity all sites are filled
2) X-ray Crystallagraphy
- structure of R group interactions of active site amino acids and substrate
3) Spectroscopic characteristics:
- changes in absorbance/ fluoresce upon mixing to substrate and E
Enzyme Active site characteristics
1) 3D cleft formed by catalytic group-R groups that interact from a vast area on linear protein and causes the protein to form to tertiary structure
2) sepresents small amount of Total V
- remaining amino acids serve as scaffolding
3) creates a unique microenvrioment
- disclude h20 so create NONpolar enviroment
- Polar amino acids attain “special” properties
4) Binds substrate to enzyme by weak interactions: hydrophobic, H-bondnig, Van Der waals NOT COVALENT
5) has specificity of binding dependant on arrangement of atoms
- lock and key
- induced fit
Basic Principles to stabilize transition States
BE CABAM
1) Binding Energies
2) Covalent catalysis
- active site contains a reactive group (nu-)that becomes covalently attached to substrate during the rxn
3) Generalized Acid/Base catalysis-molecule serves as a proton donor and receiver (His)
4) Catalysis by Approximation-2 substrates brought close to each other
5) Metal Ion Catalysis
Oxyanion Hole
Stabilizes the tetrahedral intermediate of carbonyl carbon by stabilizing the negative charge on oxygen
-hydrogen bonding of H-N of peptide backbone
Sigmoidal Curve activity in vivo
As substrate conc increases more enzyme binds to substrate and are transformed into R state, increasing the ability to bind even more substrate
isozymes
or isoenzymes
Fat soluble vitamins
FAT=Keisha Even Dick Aye? A -coenzyme; vison growth reproduction; liver D -1,25-dihydroxy-cholecalciferol -absorption of calcium and P E -none -lipid antioxidant
K
Water soluble vitamins
Connor Balls NEED Water
C-ascorbic acid
-none
-hydroxylation; antioxidant