Module 2 Flashcards
What is the function of basophils?
Inflammatory/ allergic reactions, supplement mast cells
What are the functions of eosinophils?
Inflammatory and allergic reactions, phagocytosis of antibody/ antigen complexes and fight parasites
What are the function of monocytes?
Develop to macrophages when recruits to tissue
2 types of lymphocytes?
T and B cells
Name 3 peripheral RBC proteins?
Spectrin
Ankyrin
Actin
Name 2 integral RBC proteins and their functions?
Glycoproteins A- prevents sticking
Glut 1- Glucose transport
What is the universal blood group for dogs?
DEA 4
What process determines blood group?
Glycosylation
Are RBC processes aerobic or anaerobic?
Anaerobic
What is the final product of glycolysis?
Pyruvate
How many ATP molecules does glycolysis produce?
NET 2
What is the negative allosteric inhibitor of Hb oxygen affinity?
2,3 BiPGlycerate
What is the main step in the pentode phosphate pathway?
Oxidation of Glu-6-P by NADP+ to form pentose phosphates
What are the functions of pentose phosphates?
Nucleotides or converted to glycolysis intermediates
What problems does methemoglobin (HbFe3+) cause?
No oxygen transport
Precipitates in RBC–> Heinz bodies
ROS per oxidation of lipid membranes
What is the function of a neutrophil?
Defence, phagocytosis, increase permeability of vessel walls
Metabolic causes of methemogloinemia
High oxygen and metal ions in RBC
Risk factors for methemogloinemia
Paracetamol (cats)
Onion, garlic (dogs)
Rye grass, nitrate fertilisers (cattle)
Maple leaf (horses)
What are the clinical signs of methemogloinemia?
Cyanosis (purple) Exercise intolerance Vomiting Chocolate brown blood Anameia
What can reduce metHb back to Hb?
GSH (reduced glutathione)
What molecules make up heme group?
C,H,O,N and Fe atom
Hb structure?
Protein and heme group
How many binding sites does the Fe atom have and to what does it bind?
4 N rings and 2 oxygen molecules
Where is myoglobin stored?
Skeletal muscles
How many oxygen molecules can Hb Bind to?
4
How many molecule of oxygen can myoglobin bind?
1
What is an allosteric protein?
One that changes shape/ ligand affinity when bound by small molecules and oxygen
Name an allosteric protein?
Haemoglobin
Does deoxy Hb or oxy Hb have higher affinity for oxygen?
Oxy Hb
What has higher affinity for oxygen: myoglobin or Haemoglobin?
Myoglobin
What is the effect of CO2 as an allosteric effector of oxygen binding to Hb?
Decrease Hb affinity for oxygen leading to release of oxygen and dissociation curve to right
A defect in which gene causes sickle cell anaemia?
Beta globin gene
In which condition does HbS precipitate inside RBCs and become stuck leading to the lysis of vessels?
Sickle cell anaemia
How many base substitutions cause HbS?
1
What is one advantage of HbS?
Resistance to malaria
What is the principal metabolic cause of jaundice?
High levels of free bilirubin in plasma
When is bilirubin produced?
During heme degradation
How is bilirubin usually removed?
Binds to album and transported to liver then converted to bilirubin diglucoronide and excreted as bile
What does jaundice suggest?
Excessive RBC breakdown
Decreased albumin
Impaired liver fxn
Obstruction of bile duct
Name main types of blood cells
Erythrocytes, Lymphocytes and Platelets
Function of erythrocytes?
Transport oxygen
Function of lymphocytes?
Protect against infection
Function of platelets?
Clotting
What proteins does plasma contain?
Albumin,
Immunoglobulins,
Metal ion binding proteins
Hormone binding proteins
What are the three metal ion binding proteins?
Albumin, Transferrin and Ceruloplasmin
What does ceruloplasmin transport?
Copper
What does albumin transport and what nature are these molecules?
fatty acids and sterols (hydrophobic), drugs (hydrophobic), bilirubin (hydrophobic & toxic)
Which substance is an osmotic regulator, can be broken down to AA’s during malnutrition and decreases during kidney disease and parasitic infections?
Albumin
What bond is present between the carboxylic group and amino group of an amino acid?
peptide
Name the 6 hydrophobic AA’S?
Glycine (G) (most simple) Alanine (A) Valine (V) Leucine (L) Phenylalanine (F) -aromatic Tryptophan (W)- aromatic
Hydrophilic, charged and polar AAs?
Asparatate (D) Glutamate (E) Lysine (K) Arginine (R) Histidine (H)
Hydrophilic, uncharged and polar AAs?
Asparagine (N) Glutamine (Q) Serine (S) Threonine (T) Cysteine (C)
Bonding in primary protein structure?
peptide
Bonding in secondary protein structure?
hydrogen
Features of alpha helixes?
H bonding between CO and NH 4 residues away
3.6 amino acids per turn of helix
Features of beta sheets?
H bonding between CO and NH on different polypeptide strands
Strands can run in the same direction (parallel sheets) or different directions (anti-parallel sheets)
Tertiary protein structure?
Weak, non covalent interactions
Responsible for folding
Disulphide binding between cysteine residues- stong
What are terameric proteins?
2 or more separate polypeptide chains
Define a conservative substitution?
Codon still codes for same AA
Define a radical substition and give an example?
Codon codes for different AA
E.g Sickle cell anameia
Describe the structure of collagen?
Collagen is made of a collagen triple helix
3 collagen fibres intertwined, 3 AA per turn
Every third amino acid is Gly
What bonds stabilise the structure of collagen?
Hydrogen
Describe scurvy.
Vitamin C deficiency–> less hydroxylation of proline –> fewere H bonds –>collagen unstable
Describe the features of globular proteins?
a lot of alpha helices
a lot of 3Y structure with lots of R group interactions,
non-structural proteins
ligand binding sites