Basic Genetics

Flora Gunn
Mind Map by Flora Gunn, updated more than 1 year ago
Flora Gunn
Created by Flora Gunn almost 5 years ago
3
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Description

Veterinary Biosciences Mind Map on Basic Genetics , created by Flora Gunn on 12/04/2016.

Resource summary

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