DISSOCIATION OF OXYGEN FROM HEMOGLOBIN from http://users.primushost.com/~straub/labsk_hgbdis.htm Natural oxygen transport is mediated by cell-bound hemoglobin, a protein that bonds to up to four oxygen molecules. The affinity of hemoglobin for oxygen increases with the number of oxygen molecules bound, leading to the dissociation curve seen at right. The result is an oxygen transport system that efficiently binds and releases oxygen, depending on the oxygen partial pressure. Artificial blood, more accurately known as blood substitutes, mimics some of the functions of blood. Current blood substitutes under testing are capable of passable levels of oxygen transportation, and volumetric expanders have been available for many years. The first recorded blood transfusions data back to the 17th century, but all attempts were disasters until blood typing in the early 1900s. Blood classifications allowed for transfusions without immediate acute immunologic response from patients. This website ©2007 Rachel Griffith, Benjamin Groisser, Rachel Lipman, Timothy Nolan, Austin Ranz