Hemoglobin Structure, Types, and Oxygen Dissociation Vocabulary

0.0(0)
Studied by 0 people
call kaiCall Kai
Locked
learnLearn
examPractice Test
spaced repetitionSpaced Repetition
heart puzzleMatch
flashcardsFlashcards
GameKnowt Play
Card Sorting

1/11

flashcard set

Earn XP

Description and Tags

Vocabulary flashcards covering the structural components of hemoglobin, developmental hemoglobin types, metabolic pathways, oxygen dissociation curve shifts, and abnormal hemoglobins based on lecture transcript notes.

Last updated 5:54 PM on 9/8/26
Name
Mastery
Learn
Test
Matching
Spaced
Call with Kai
Chat

No analytics yet

Send a link to your students to track their progress

12 Terms

1
New cards

Heme

The iron-containing structure composed of iron in the ferrous form (Fe2+\text{Fe}^{2+}) bound to protoporphyrin nine.

2
New cards

Adult Hemoglobin (Hb A)

The predominant form of hemoglobin in adults, composed of heme combined with two alpha globin chains and two beta globin chains.

3
New cards

Fetal Hemoglobin (Hb F)

A form of hemoglobin composed of two alpha chains and two gamma chains (α2γ2\alpha_2\gamma_2) that predominates before birth and transitions to adult hemoglobin after delivery.

4
New cards

Embryonic Hemoglobin

Early developmental forms of hemoglobin produced before birth, specifically Gower 1, Gower 2, and Portland.

5
New cards

Luber-Luberine Rapivor Pathway

The metabolic pathway in red blood cells that produces 2,3-DPG, which alters hemoglobin conformation to facilitate carbon dioxide pickup and oxygen release.

6
New cards

Oxygen Dissociation Curve

A sigmoid or S-shaped curve that describes the relationship between partial pressure of oxygen and the binding or release of oxygen by hemoglobin.

7
New cards

Right Shift

A shift in the oxygen dissociation curve where oxygen is loosely bound to hemoglobin (Righty Loosey) and released easily, caused by decreased pH, increased temperature, or increased 2,3-DPG.

8
New cards

Left Shift

A shift in the oxygen dissociation curve where oxygen is tightly bound to hemoglobin (Lefty Tighty) and not released easily, caused by increased pH, decreased temperature, decreased 2,3-DPG, or stored blood depletion.

9
New cards

Methemoglobin

An abnormal form of hemoglobin containing iron in the ferric state (Fe3+\text{Fe}^{3+}) rather than the ferrous state, rendering it incapable of binding oxygen and causing a right shift.

10
New cards

Carboxyhemoglobin

An abnormal form of hemoglobin that has a high affinity for carbon monoxide (CO) rather than oxygen, causing a right shift in the oxygen dissociation curve.

11
New cards

Sulfhemoglobin

An abnormal form of hemoglobin created by exposure to sulfonamides or sulfa-containing drugs that has a reduced affinity for oxygen, leading to a right shift.

12
New cards

Mature Red Blood Cells

Circulating red blood cells that generate ATP, methemoglobin reductase, and 2,3-DPG, but do not produce hemoglobin, as hemoglobin synthesis occurs in the bone marrow.