AC
AnkiCollab
AnkiCollab
Sign in
Explore Decks
Helpful
Join Discord
Download Add-on
Documentation
Support Us
Notes in
✧ Hemoglobin
To Subscribe, use this Key
beer-georgia-london-nitrogen-lake-louisiana
Status
Last Update
Fields
Published
01/14/2024
O2 is carried in blood in two forms: {{c2::dissolved}} (2%) or {{c1::bound to hemoglobin}} (98%)
Published
01/14/2024
Hemoglobin is a globular protein consisting of {{c1::four}} subunits
Published
01/14/2024
Each subunit of hemoglobin contains a(n) {{c1::heme}} moiety, which is a(n) {{c2::iron}}-binding porphyrin, and a polypeptide chain
Published
01/14/2024
Iron in hemoglobin is normally in the {{c1::ferrous (Fe2+)}} state
Published
01/14/2024
If the iron in hemoglobin is in the {{c1::ferric (Fe3+)}} state, it is called {{c2::methemoglobin}}
Published
01/14/2024
Methemoglobin (Fe3+) binds O2 much {{c1::less::more/less}} readily than hemoglobin (Fe2+)
Published
01/14/2024
Methemoglobin has a(n) {{c1::increased}} affinity for {{c2::cyanide}} relative to hemoglobin
Published
01/14/2024
{{c1::Methemoglobinemia}} may present with {{c3::cyanosis}} and {{c2::chocolate}}-colored blood
Published
01/14/2024
Induced-{{c1::methemoglobinemia}} (i.e. {{c3::nitrites}} followed by {{c3::thiosulfate}}) may be used to treat {{c2::cyanide}} poisoning
Published
01/14/2024
Methemoglobinemia can be treated with {{c1::methylene blue}} or {{c2::vitamin C}}
Published
01/14/2024
What two drug classes are associated with methemoglobinemia? {{c1::Nitrates (and nitrites) & Sulfa drugs}}
Published
01/14/2024
Polluted/high altitude H2O may contain {{c1::nitrites}}, which can cause methemoglobinemia
Published
01/14/2024
{{c1::Benzocaine}} is a local anesthetic that may cause methemoglobinemia in toxic doses
Published
01/14/2024
Methemoglobinemia is associated with {{c1::decreased}} SaO2, {{c1::decreased}} O2 content, and {{c1::normal}} PaO2
Published
01/14/2024
Most adult hemoglobin is composed of 2 {{c1::α}} and 2 {{c1::β}} subunits; known as {{c2::HbA}}
Published
01/14/2024
Fetal hemoglobin, known as {{c2::HbF}}, is composed of 2 {{c1::alpha}} and 2 {{c1::gamma}} subunits
Published
01/14/2024
Fetal hemoglobin (HbF) has a much {{c1::higher}} binding affinity for O2 than adult hemoglobin (HbA)
Published
01/14/2024
Why must fetal hemoglobin have a much higher O2 binding affinity than HbA? {{c1::Drives O2 diffusion across placenta from mother to fetus}}
Published
01/14/2024
The increased O2 binding affinity of fetal hemoglobin results from {{c1::decreased}} affinity of HbF for {{c2::2,3-BPG}}
Published
01/14/2024
Hemoglobin exists in two forms: {{c1::taut}} (deoxygenated) and {{c1::relaxed}} (oxygenated)
Published
01/14/2024
The {{c2::taut}} form of hemoglobin has a(n) {{c1::low}} affinity for O2
Published
01/14/2024
The {{c2::relaxed}} form of hemoglobin has a(n) {{c1::high}} affinity for O2
Published
01/14/2024
The {{c1::taut}} form of hemoglobin is found in most tissues
Published
01/14/2024
The {{c1::relaxed}} form of hemoglobin is found in the respiratory tract
Published
01/14/2024
Normally 1g of hemoglobin can bind {{c1::1.34}} mL of O2
Published
01/14/2024
Normally there is ~{{c1::15}} g/dL of hemoglobin in blood
Published
01/14/2024
The O2-binding capacity of blood is {{c1::20.1}} mL O2/ 100 mL blood
Published
01/14/2024
What equation may be used to calculate the O2 content of blood?O2 content = {{c1::(1.34 * Hb * SaO2) + (0.003 * PaO2)}}
Published
01/14/2024
Decreased hemoglobin (e.g. anemia) is associated with {{c1::normal}} SaO2, {{c1::decreased}} O2 content, and {{c1::normal}} PaO2
Published
01/14/2024
What equation may be used to calculate O2 delivery to tissues? O2 delivery = {{c1::cardiac output * O2 content of blood}}
Published
01/14/2024
The {{c2::sigmoidal}} shape of the oxygen-hemoglobin dissociation curve is due to {{c1::positive cooperativity}} (increased affinity for each sucessiv…
Published
01/14/2024
A(n) {{c2::hemo}}-globin molecule has the potential to bind {{c1::4}} O2 molecule(s)
Published
01/14/2024
A(n) {{c2::myo}}-globin molecule has the potential to bind {{c1::1}} O2 molecule(s)
Published
01/14/2024
The {{c1::P50}} of the oxygen-Hb dissociation curve is the Po2 at which hemoglobin is 50% saturated
Published
01/14/2024
The oxygen-Hb dissociation curve is roughly flat when the Po2 is between {{c1::60}} and {{c1::100}} mmHg
Published
01/14/2024
Does the oxygen-myoglobin dissociation curve have a sigmoidal shape? Why?{{c1::No, myoglobin is monomeric (no positive cooperativity)}}
Published
01/14/2024
Shifts of the O2-Hb dissociation curve to the {{c1::right}} occur when there is {{c2::decreased}} affinity of hemoglobin for O2
Published
01/14/2024
Shifts of the O2-Hb dissociation curve to the {{c1::right}} cause {{c2::increased}} unloading of O2 at tissues
Published
01/14/2024
Increased pCO2 and resulting decrease of pH enhancing the release of O2 from hemoglobin is called the {{c1::Bohr}} effect
Published
01/14/2024
{{c1::Increases}} in Pco2 cause the O2-hemoglobin dissociation curve to shift to the {{c2::right}}
Published
01/14/2024
{{c1::Decreases}} in pH cause the O2-hemoglobin dissociation curve to shift to the {{c2::right}}
Published
01/14/2024
{{c1::Increases}} in temperature cause the O2-hemoglobin dissociation curve to shift to the {{c2::right}}
Published
01/14/2024
{{c1::Increases}} in 2,3-BPG cause the O2-hemoglobin dissociation curve to shift to the {{c2::right}}
Published
01/14/2024
2,3-BPG decreases the affinity of hemoglobin for O2 by binding to hemoglobin {{c2::β}} chains
Published
01/14/2024
How do levels of 2,3-BPG change at high altitudes? {{c1::Increased}}
Published
01/14/2024
2,3-BPG increases under {{c1::hypoxic}} conditions (e.g. high altitude)
Published
01/14/2024
High altitudes indirectly cause the O2-hemoglobin dissociation curve to shift to the {{c2::right}}
Published
01/14/2024
Factors that shift the O2-Hb dissociation curve to the {{c1::right}} favor the {{c2::taut}} form of hemoglobin
Published
01/14/2024
Shifts of the O2-Hb dissociation curve to the {{c1::left}} occurs when there is {{c2::increased}} affinity of hemoglobin for O2
Published
01/14/2024
Shifts of the O2-Hb dissociation curve to the {{c1::left}} cause {{c2::decreased}} unloading of O2 at tissues
Published
01/14/2024
{{c1::Decreases}} in Pco2 cause the O2-hemoglobin dissociation curve to shift to the {{c2::left}}
Published
01/14/2024
{{c1::Increases}} in pH cause the O2-hemoglobin dissociation curve to shift to the {{c2::left}}
Published
01/14/2024
Decreases in temperature cause the O2-hemoglobin dissociation curve to shift to the {{c2::left}}
Published
01/14/2024
{{c1::Decreases}} in 2,3-BPG cause the O2-hemoglobin dissociation curve to shift to the {{c2::left}}
Published
01/14/2024
{{c1::Increases}} in hemoglobin F cause the O2-hemoglobin dissociation curve to shift to the {{c2::left}}
Published
01/14/2024
{{c1::Carboxyhemoglobin}} is a form of hemoglobin bound to {{c2::CO}} in place of O2
Published
01/14/2024
Carbon monoxide binds competitively to Hb and with 200-250x {{c1::greater}} affinity than O2
Published
01/14/2024
Carboxyhemoglobin causes the O2-hemoglobin dissociation curve to shift to the {{c2::left}}
Published
01/14/2024
Carboxyhemoglobin heme groups not bound by CO have a(n) {{c1::increased}} affinity for O2
Published
01/14/2024
Carboxyhemoglobin causes {{c2::decreased}} unloading of O2 at tissues
Published
01/14/2024
Carboxyhemoglobin causes {{c1::decreased}} O2-binding capacity
Published
01/14/2024
Carboxyhemoglobinemia (CO poisoning) may be treated with {{c1::100% O2}} and {{c2::hyperbaric O2}}
Published
01/14/2024
Carboxyhemoglobinemia is associated with {{c1::decreased*}} SaO2, {{c1::decreased}} O2 content, and {{c1::normal}} PaO2
Published
01/14/2024
What is the hemoglobin concentration in carboxyhemoglobinemia?{{c1::Normal}}
Published
01/14/2024
CO2 binding to hemoglobin favors the {{c1::taut}} form, thus {{c1::reducing}} Hb affinity for O2
Published
01/14/2024
Hypoxia may be caused by {{c1::carbon monoxide}} poisoning, which decreases the O2 content of blood
Published
01/14/2024
1,3-bisphosphoglycerate may be converted to {{c1::2,3-BPG}} via the enzyme bisphosphoglycerate mutase in red blood cells
Published
01/14/2024
In red blood cells, lack of NADH impairs the ability to reduce Fe3+ to Fe2+, predisposing to {{c1::methemoglobinemia}}
Published
01/14/2024
Vitamin {{c1::C}} is used as an ancillary treatment for {{c2::methemoglobinemia}}
Published
01/14/2024
One normal type of hemoglobin is {{c2::HbF}} which is composed of two {{c1::α}} and two {{c1::γ}} chains
Published
01/14/2024
One normal type of hemoglobin is {{c2::HbA}} which is composed of two {{c1::α}} and two {{c1::β}} chains
Published
01/14/2024
One normal type of hemoglobin is {{c2::HbA2}} which is composed of two {{c1::α}} and two {{c1::δ}} chains
Published
01/14/2024
{{c2::Benzocaine}} is a local anesthetic that is associated with {{c1::methemoglobinemia}} as an adverse effect
Published
01/14/2024
What skin appearance is classically seen in carbon monoxide poisoning? {{c1::Cherry-red appearance}}
Published
01/14/2024
Methemoglobinemia can be treated by {{c1::methylene blue}} and {{c2::vitamin C}}
Published
01/14/2024
Methylene Blue works for the treatment of methemoglobinemia by {{c1::reducing Fe3+ to Fe2+}}
Published
01/14/2024
Carbon monoxide poisoning can be treated with {{c1::100% O2}} or hyperbaric O2
Status
Last Update
Fields