(P) Week 3: RBC function Part 2 Flashcards
What is the main objective of the hexose monophosphate pathway
produce reduced glutathione
____________ protects the molecular structure of our hemoglobin by acting against accumulating oxidants and peroxides which destroys cells and deteriorate hemoglobin
glutathione
What is the first enzyme involved in the Hexose monophosphate pathway
glucose-6-phosphate dehydrogenase
the hemoglobin of individuals with _______________ deficiency is solid, unstable, will crystallize, and precipitate in the cytoplasm of the red cell
G6PD deficiency
a large body formation / inclusion seen within rbcs associated with G6PD deficiency
Heinz bodies
T or F
Heinz bodies are specific to G6D
F (it is also seen in other unstable hgb problems)
2 forms of the hemoglobin
T form (Tense)
R form (Relax)
this form of hgb is unoxygenated
T form
this form of hgb is oxygenated
R form
at what angle does hgb twist at in order to let 2,3-DPG molecule exit, so that oxygen may enter and bind to the heme
15 deg
When the oxygen is delivered to the tissues and organ, hgb twists at what angle to squeeze out the remaining oxygen?
zero deg
T or F
Hgb F, composed of 2 alpha and 2 beta globin chains may enter to either T or R form
F (Hgb A1)
What form of Hgb twists to a zero deg angle
T form
what form of Hgb twists to a 15 deg angle?
R form
what is the normal blood pH
7.35-7.45
during hypoventilation we suffer from _________ (acidosis / alkalosis)
acidosis
less breathing = more CO2 on bloodstream
co2 binding with water to create carbonic acid makes the blood (acidic / alkaline)
acidic
during hyperventilation we suffer from (acidosis / alkalosis)
alkalosis
decreased CO2 in the blood leads to (acidosis / alkalosis)
alkalosis
this mechanism of our bodies does it best to compensate and return our blood pH within normal levels (7.35 - 7.45)
compensatory mechanism
T or F
Lungs, Kidneys, and RBC itself aid in maintaining blood pH at normal levels
T
what is the partial pressure of residual oxygen in the RBC
40 mmHg
T or F
even if there’s still residual oxygen in the RBC, they may still be referred to as unoxygenated RBC
T
What is the partal pressure of the lugs
100-120 mmHg
As you go to a place with a higher altitude, the oxygen pressure in the lungs ___________causing a person to have a difficulty in breathing
decreases
oxygen in the lungs is able to enter the RBC via what process?
simple diffusion
lungs (high pressure) to RBC (low pressure)
oxygenated RBC’s oxygen pressure is at
100 mmHg
What is the oxygen saturation of oxygenated RBCs with 100 mmHg of pressure
95-97%
how many atoms of oxygen does an oxygenated Hgb carry?
4 atoms
whenever oxygen (____ charged) is given off to the tissue, hemoglobin may now assume a ______ charge
positive charge
negative charge
what enzyme aids the binding of CO2 and H2O?
carbonic anhydrase
remember: CO2 + H2O = H2CO3 / carbonic acid
what does the hgb’s negative charge attracts from the tissue, causing for its acidity to slightly increase?
one hydrogen atom
____________ is formed due to the loss of one hydrogen atom in the carbonic acid
bicarbonate (HCO3)
a phenomenon described as the release of oxygen from the Hgb to the tissue, and the binding of the H+ ion
Bohr effect
T or F
acidosis = increased bicarbonate
f (increased carbon dioxide)
T or F
In cases of alkalosis, the Hgb holds onto the oxygen to prevent the absorption of a H+ molecule, promoting the further production of carbonic acid as it will not be converted to bicarbonate
T
term used for when the blood loses its negative charge
chloride shifting
T or F
carbon dioxide directly binds to the Hgb
f (it shouldn’t directly bind as it will create bubbles in the blood because it’s a gas)
T or F
in the lungs, Hgb is more attracted to CO2
F (oxygen)
the break down of carbonic acid into water and Co2, by carbonic anhydrase, is done where?
alveoli
what are the stages do CO2 go through in order to be released outside our body
bicarbonate -> carbonic acid -> (broken down by carbonic anhydrase) -> carbon dioxide to be released
70% of carbon dioxide that is carried in the lungs is in the
plasma bicarbonate
20% of carbon dioxide that is carried
in the lungs is in the
erythrocyte bicarbonate
The remaining 10% of carbon dioxide is transported into two other ways.
a. dissolved and binds with the n-terminal to amino acid from ________________
b. The other 5% is transported in other solutions
carbaminohemoglobin
the phenomenon that prevents CO2 in the lungs to go back to the Hgb
Haldane effect
T or F
CO2 is more attracted to the hemoglobin if it is unoxygenated
T
____________ is inserted into your finger to measure oxygen saturation
oximeter
how is the normal curve of oxygen illustrated as in oxygen dissociation curve?
solid line
if you’ve reached 50% oxygen saturation, how much pressure is needed to reach normal levels of o2 saturation?
26-27 mmHg
What is the normal pressure needed to reach 100% o2 saturation?
60-80 mmHg of pressure
what type of curve is produced in the oxygen dissociation curve when it has reached a plateau?
sigmoid curve
shifting to which side in the oxygen dissociation curve indicate that your body needs more oxygen?
to the right
T or F
the oxygen dissociation curve will shift to the left when your body is in acidosis
F (right)
An increased release of ______ to the tissue causes the oxygen dissociation curve to shift to the right
oxygen
a/an __________ release of oxygen to the tissue causes the oxygen dissociation curve to shift to the left
decreased
shift to the left or right?
hyperthyroidism
shift to the right
shift to the left or right?
hypothyroidism
shift to the left
shift to the left or right?
hypercapnia
shift to the right
shift to the left or right?
low blood pH
shift to the right
shift to the left or right?
hypocapnia
shift to the left
hyperthermia
shift to the right
shift to the left or right?
high blood pH
shift to the left
shift to the left or right?
high 2,3 DPG level
shift to the right
shift to the left or right?
hypocapnia
shift to the left
shift to the left or right?
low 2,3 DPG level
shift to the left
shift to the left or right?
methemoglobin
shift to the right
shift to the left or right?
Hgb F
shift to the left
shift to the left or right?
carboxyhemoglobin
shift to the left
shift to the left or right?
hemoglobin chesapeake
shift to the left
shift to the left or right?
hemoglobin s
shift to the right
shift to the left or right?
hemoglobin kansas
shift to the right
disease associated with the formation of sulfhemoglobin
clostridium perfringens infection
The counterpart of Hgb kansas
hgb chesapeake
facilitates the binding of the hgb in the tissue where the pCO2 is high, an the release of carbon dioxide in the lungs when pCO2 is low
Haldane effect
protein similar to hgb, it has globin chains and heme, and oxygen also binds to it, but it has a different structur
myoglobin
composed of single chain of 154 amino acids that forms eight alpha helices and one heme or protoporphyrin IX
myoglobin
myoglobin molecular weight
17,000 daltons
hgb molecular weight
64,000 daltons
hemoglobin : sigmoidal
myoglobin : ________________
hyperbolic
2 forms of myoglobin
deoxymyoglobin
oxymyoglobin
T or F
Myoglobin immediately releases the oxygen
F (does not, in fact, it binds strongly to the oxygen)
T or F
myoglobin releases the oxygen ring only if the oxygen tension in the muscle is severely decreased
T
clinical use of myoglobin
identification of rhabdomyolysis
other name for rhabdomyolysis
crush syndrome
________ levels of myoglobin in the blood indicates rhabdomyolysis / crush syndrome
increased
Parasite that can destroy the muscles, increases myoglobin levels in the blood
trichinella spiralis
type of hemolysis wherein macrophages kill senile red cells in the spleen
extravascular hemolysis
type of hemolysis where senile rbcs die in the circulation
intravascular hemolysis
condition secondary to red cells dying earlier than the expected life span (120 days)
hemolytic anemia
pls study heme catabolism again
kung ayaw mo edi wag *eyeroll
what is the product of heme catabolism
bilirubin
this becomes unconjugated bilirubin in extravascular hemolysis
porphyrin
what aids unconjugated bilirubin to travel to the liver
albumin
proteins responsible to carry the hemoglobin for it to be converted to biliverdin nd bilirubin
haptoglobulin
hemopexin
metheme
bacteria in the large intestine will convert bilirubin to either
stercobilin or urobilinogen
these parameter(s) increase in cases of hemolytic anemia
bilirubin and methemalbumin
pathway that anaerobically generates ATP
EMP
parameter(s) that are decreased in cases of hemolytic anemia
haptoglobulin and hemopexin
What HMP shunt product detoxify peroxides
NADPF and reduced glutathione
if you’re a concrete sequential worker
give nath a kith
