Human Physiology · MU Plovdiv

43. Transport of O2 in the blood. Oxyhemoglobin dissociation curves. Oxygen exchange in the lungs and tissues. Transport of CO2 in the blood. Carbon dioxide exchange in the lungs and tissues.

Inside: 8 sections · 10 labelled pictures · 29 flashcards · 8 min

Topic 43 of 69 in the MU Plovdiv syllabus for Human Physiology (Dental Medicine, Year 2). The free AceMed note covers it in 7 sections, about 1,111 words (8 min of reading), with 29 flashcards.

In this note

  1. Transport of oxygen in the blood. Oxyhemoglobin dissociation curve. Oxygen delivery to the tissues.
  2. Forms of Oxygen in Blood
  3. Oxyhemoglobin Dissociation Curve.
  4. Oxygen Delivery to Tissues
  5. Recap Questions
  6. Transport of carbon dioxide in the blood. Dissociation curve of carbaminehemoglobin.
  7. Forms of CO2 Transport in the Blood:

Forms of Oxygen in Blood

Oxygen is transported in the blood in two forms:

  • Dissolved O2: A small fraction (around 2%) of total oxygen is dissolved directly in the blood plasma. This dissolved oxygen is crucial as it is the only form that exerts partial pressure, driving oxygen diffusion across membranes.
  • O2 Bound to Hemoglobin: The vast majority (around 98%) of oxygen is transported bound to hemoglobin, a protein found inside red blood cells (erythrocytes). Hemoglobin consists of four subunits (two α and two β chains), each containing a heme group with an iron atom. Each iron atom can reversibly bind one oxygen molecule, allowing a single hemoglobin molecule to carry up to four oxygen molecules. This binding of oxygen to hemoglobin is rapid and reversible. When oxygenated, it is called oxyhemoglobin, and when deoxygenated, it's called deoxyhemoglobin.

♦ Haemoglobin: Haemoglobin is the molecule that allows O2 to bind and dissociate in the blood, One molecule of Haemoglobin (Hb) binds 4 molecules of O2.

There are 3 main types of haemoglobin.

  • Haemoglobin A, is composed of 2 α-chains and 2 β-chains, 95%
  • Haemoglobin A2, is composed of 2 α-chains and 2 δ-chains, 1,5-3,5%
  • Haemoglobin F, is composed of 2 α-chains and 2 γ-chains, it is found in the fetus and has a higher affinity for O2. (Haemoglobin S is found in patients with sickle-cell anomia, the problem lies in a mutation of the two β-chains).

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