Blood
About 98.5% of the oxygen in a sample of arterial blood in a healthy human breathing air at sea-level pressure is chemically combined with the hemoglobin. About 1.5% is physically dissolved in the other blood liquids and not connected to hemoglobin. The hemoglobin molecule is the primary transporter of oxygen in mammals and many other species (for exceptions, see below). Hemoglobin has an oxygen binding capacity between 1.36 and 1.40 ml O per gram hemoglobin, which increases the total blood oxygen capacity seventyfold, compared to if oxygen solely were carried by its solubility of 0.03 ml O per liter blood per mm Hg partial pressure of oxygen (about 100 mm Hg in arteries).
Common octopus
The blood of the octopus is composed of copper-rich hemocyanin which is less efficient than the iron-rich hemoglobin of vertebrates and thus does not increase oxygen affinity to the same degree. Oxygenated hemocyanin in the arteries binds to CO, which is then released when the blood in the veins is deoxygenated. The release of CO into the blood causes it to acidify by forming carbonic acid. The Bohr effect explains that carbon dioxide concentrations affect the blood pH and the release or intake of oxygen. The Krebs cycle uses the oxygen from the blood to break down glucose in active tissues or muscles and releases carbon dioxide as a waste product, which leads to more oxygen being released. Oxygen released into the tissues or muscles creates deoxygenated blood which returns to the gills in veins. The two brachial hearts of the octopus pump blood from the veins through the gill capillaries. The newly oxygenated blood drains from the gill capillaries into the systemic heart where it is then pumped back throughout the body.