Hemoglobin and iron metabolism. Flashcards
hemoglobin LIST
structures
functions
types
clincials
measurements
she
found
two
cute
monsters
hemoglobin - structure 1
hemoglobin is a tetramer protein meaning made of 4 polypeptide chains
HemoglobinA = x2 alpha subunits
HemoglobinB = x2 beta subunits
hemoglobin - structure 2
1 hemoglobin = 4 subunits = 4 heme group = iron centre = x1 oxygen binded
hemoglobin - function 1
OXYGEN TRANSPORT
hemoglobin + oxygen = oxyhemoglobin (lungs)
reaching tissues/ organs
hemoglobin - function 2
CARBON DIOXIDE TRANSPORT
hemoglobin + carbon dioxide = carbo-amino-hemoglobin
- reaches lungs
hemoglobin - function 3
BUFFERING
hemoglobin acts a as buffer to maintain correct blood pH levels in terms of H+/HCO3=
hemoglobin - function 4
bohr effect 1
BOHR EFFECT
- more co2 -> diffuses into blood
hemoglobin - function 4
bohr effect 2
- co2 + h2o = h2co3 = lowers blood pH
hemoglobin - function 4
bohr effect 3
- hemoglobin has less affinity to bind to oxygen, so oxygen is left behind + released into tissues
hemoglobin - function 4
bohr effect 4
- oxygen dissociation curve turns right
hemoglobin - function 4
bohr effect 5
ensures active tissues producing more co2 get more o2-> to improve efficiency of o2 transport
hemoglobin - function 5
HALDANE EFFECT
when hemoglobin binds to oxygen = changes shape
Hb now so less affinity for co2
Hb better at picking up co2 to be taken back to lungs
hemoglobin - type 1
ADULT HEMOGLOBIN
- HemoglobinA = x2 chains
- HemoglobinB = x2 chains
hemoglobin - type 2
FETAL HEMOGLOBIN
- HemoglobinA = x2 chains
- HemoglobinF = x2 chains
HbF has higher affinity for oxygen than HbA = oxygen transfer from mother -> foetus
hemoglobin - type 3
SICKLE HEMOGLOBIN
HemoglobinS
- abnormal variant for sickle cell anemia
- caused by point mutation of HBB gene on chromosome 11
- valine overtakes glutamic acid on position 6 of HemaglobinB chain