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7189691
Basic Genetics
Descrição
Veterinary Biosciences Mapa Mental sobre Basic Genetics , criado por Flora Gunn em 04-12-2016.
Sem etiquetas
veterinary biosciences
Mapa Mental por
Flora Gunn
, atualizado more than 1 year ago
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Criado por
Flora Gunn
quase 8 anos atrás
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Resumo de Recurso
Basic Genetics
Protein sequence from amino to carboxyl end N-C
Primary Structure: no interactions or stabilising bonds
Secondary Structure: H bonding between carbonyl oxygen and amide hydrogen
Tertiary Structure: myoglobin and Haemoglobin
Quaternary Structure: 4 subunits interacting. Has 4y structure
PROTEIN PURIFICATION - BY SIZE
ULTRAFILTRATION
Small molecules forced through membrane by pressure or centrifugation
DIALYSIS
Semi-permeable membrane, small molecules pass out
GEL FILTRATION
Large molecules out first and large amounts of protein can be separated
PROTEIN PURIFICATION - BY CHARGE
net +ve charge binds to -ve molecules
net -ve charge binds to +ve molecules
Separate in a column containing beads
ROLES OF BLOOD
Transports nutrients to tissues, including O2
Removes waste products
Protects against infection
Repair of tissue damage
BLOOD CELLS
Erythrocytes (RBCs) Transports oxygen
Leukocytes (WBCs) Lymphocytes, monocytes and granulocytes. Protects against infection
Platelets (thrombocytes) Cell fragments and blood clotting
ALBUMIN
3 Domains
Free Cys
Alpha helix, no beta sheet
No glycolysation
Most abundant
Important in solubilisation, transport and removal of hydrophobic molecules in hydrophilic environment of plasma
ALBUMIN IN OSMOTIC REGULATION
High concentration in plasma
Prevents tissue taking up excess water
Osmolarity of plasma decreases (less protein)
Water enters tissues
OEDEMA - swelling
BLOOD CLOTTING CASCADE
As a result of damage to blood vessels
Prevents excess blood loss
2 STEP PROCESS
1) Platelet Agreggation
Platelets adhere to vessel wall and aggregate. Forms 1y plug and needs to be stabilised
2) Activation of coagulation factors
Plug stabilised by X-linking of FIBRIN and forms 2y plug
Cascade is tightly regulated and zymogen activated
Catalytic proteases activate next factor
Controlled by inactivation of proteases by inhibitors
Large amplification of response to damage = rapid response
HAEMOGLOBIN
4 sub units
much alpha helix
4 haem groups
Binds oxygen in lungs as CO2 released, pH is raised and allosteric action results in high affinity
Carries oxygen to tissues where pH is lower and HCCO2 inhibits binding by allosteric action
Oxygen transferred to myoglobin, which now has higher affinity
ACUTE PHASE PROTEINS
C - Reactive Protein (CRP)
5 units form penraxin ring
Binds to phosphoryl choline and nucleic acids
Activates complement to lyse bacteria
Scavenger for nucleic acid from cell necrosis
APP in human, dog and pig. Not in cat, horse, cow.
Serum Amyloid A (SAA)
Many hydrophobic amino acids
Involved with cholesterol transport
Antibacterial activity
4 isoforms in most species. 1+2 acute phase stimulated, 3 is produced by non-hepatic tissue in the acute phase. SAA 4 is not an APP
stimulates mucin production in intestine
Present in colostrum and milk from cows with mastitis
Class of proteins whose plasma concentrations increase or decrease in response to inflammation
Haptoglobin
2 alpha and 2 beta sub units
In ruminants forms high mol weight polymers
In ruminants, a major APP
In dog, cat, horse and pig, a moderate APP
In dog, Hp is stimulated by cortisol as well as in acute phase response
Binds strongly to free haemoglobin
Haemoglobin binding is the basis of a rapid assay
Anti-oxidant activity
Alpha 1 Acid Glycoprotein
Highly glycosylated + soluble
>40% is attached to carbohydrate
Binds to drugs + endogenous ligands
Can alter the free concentration of drugs
Shows immunomodulatory activity
Reduces bacterial spread by reducing vascular permeability
TRANSFERRIN
Transports Fe as ferric ion
Both alpha helices and beta sheets
Forms 2 different lobes, N and C terminus
Domains are held together by a short peptide with a deep hydrophobic site
FE 3+ BINDING
The amino acids binding ferric iron ion are the same for both lobes
The binding of iron also needs an anion which is usually carbonate (CO3 2-)
Binding stabilised by: Tyr 192, tyr 92, His 253 and ASP 301
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