Practice Test #2 Flashcards
What kind of therapy is needed for treating anaemia resulting from renal disease or from various other causes
Recombinant erythropoietin
What is the method of administration for Recombiant erythropoietin
Subcutaneously
How often is Recombinant erythropoietin used in treatment
three times weekly or once every 1–2 weeks or every 4 weeks
What is the main indication for Erythropoietin therapy
End-stage renal disease (with or without dialysis)
What is also needed in erythropoietin therapy
oral or intravenous iron
True or False, A high serum erythropoietin level prior to treatment is valuable in predicting an e ective response
False, Low Level
What are some common side effects for recombinant erythropoietin therapy
Side‐effects include a rise in blood pressure, thrombosis and local injection site reactions.
What hormones are necessary for effective erythropoiesis
Androgens and thy- roxine
What metals are needed in successive erythropoietin synthesis
iron and cobalt
What is the dominant haemoglobin in blood after the age of 3–6 months) c
HbA
What are the 4 polypeptide chain in Haemoglobin A
α2 β2, each with its own haem group
What are the clinical uses of erythropoietin
Anaemia of chronic renal disease
Myelodysplastic syndrome
Anaemia associated with malignancy and chemotherapy
Anaemia of chronic diseases, e.g. rheumatoid arthritis
Anaemia of prematurity
Perioperative uses
What is the main site for the protoporphyrin synthesis
Mitochondria
Where is Iron supplied from for erythropoiesis
Circulating transferrin
What synthesis occurs largely in the mitochondria
Haem
What is the key rate‐limiting enzyme in Haem Synthesis
δ‐aminolaevulinic acid (ALA) synthase
What is the coenzyme for Haem synthesis
Pyridoxal phosphate (vitamin B )
The condensation of which two compounds occurs in the biochemical reaction for haem synthesis
condensation of glycine and succinyl coenzyme A
The combination of which two compounds for Haem
Protoporphyrin combines
with iron in the ferrous (Fe2+)
True or False the contact of α1α2 β2β1 stabilises the structure of Haemoglobin
False it is, α2β2, α1β1
When O2 is unloaded β chains are pulled apart permitting the entry of which metabolite
2,3‐diphosphoglycerate (2,3‐DPG)
True or False, The entry of the metabolite in the β chains results in higher affnity of the molecule for O2.
False, lower
What is the P50 (i.e. the partial pressure of O2 at which haemoglobin is half saturated with O2) of normal blood
26.6 mmHg
What occurs with an increased affnity for O2 in a haemoglobin oxygen (O2) dissociation curve
Curve shifts to the left
True or False, The P50 will rise when there is an increase affinity for O2
False, it will fall
What causes the curve to shift to the right in a haemoglobin oxygen (O2) dissociation curve
Decreased affinity for O2
A rise in P50 is as result of
Decreased affinity for O2
In vivo, O2 exchange operates at ____ saturation in arterial blood
95%
in vivo, What is the mean arterial O2 tension
95mmHg
In vivo, O2 exchange operates at ____ in venous blood
70%
In vivo, What is the mean venous O2 tension
40 mmHg
The normal position of the curve depends on which 3 compound in the red cell
2,3‐DPG, H+ ions and CO2
What is the difference between normal Adult Hb and Fetal Hb
Fetal Hb is unable to bind 2,3 DPG
Rare abnormal haemoglobins associated with polycythaemia, will cause the oxygen dissociation curve to shift to which direction
Left
What is the name of the clinical state in which circulating haemoglobin is present with iron in the oxidized (Fe3+) instead of the usual Fe2+ state.
Methaemoglobinaemia
Where does Methaemoglobinaemia arise from
hereditary deficiency of methaemoglobin reductase deficiency or inheritance of a structurally abnormal haemoglobin (Hb M)