Search results
Results from the WOW.Com Content Network
X-ray images indicate scapholunate ligament instability when the scapholunate distance is more than 3 mm, which is called scapholunate dissociation. [7] A static scapholunate instability is generally readily visible, but a dynamic scapholunate instability can only be seen radiographically in certain wrist positions or under certain loading conditions, such as when clenching the wrist, or ...
In radiology, the Terry-Thomas sign is a scapholunate ligament dissociation on an anteroposterior view of the wrist. [1] [2] Most commonly a result of a fall on the outstretched hand , the scapholunate ligament ruptures resulting in separation of the lunate and scaphoid bones. This burst causes the scaphoid bone to dorsally rotate. [3]
Each curve corresponds to a different Hill coefficient, labeled to the curve's right. The vertical axis displays the proportion of the total number of receptors that have been bound by a ligand. The horizontal axis is the concentration of the ligand. As the Hill coefficient is increased, the saturation curve becomes steeper.
The oxygen–hemoglobin dissociation curve, also called the oxyhemoglobin dissociation curve or oxygen dissociation curve (ODC), is a curve that plots the proportion of hemoglobin in its saturated (oxygen-laden) form on the vertical axis against the prevailing oxygen tension on the horizontal axis. This curve is an important tool for ...
In chemistry, biochemistry, and pharmacology, a dissociation constant (K D) is a specific type of equilibrium constant that measures the propensity of a larger object to separate (dissociate) reversibly into smaller components, as when a complex falls apart into its component molecules, or when a salt splits up into its component ions.
The sigmoidal shape of hemoglobin's oxygen-dissociation curve results from cooperative binding of oxygen to hemoglobin. An example of positive cooperativity is the binding of oxygen to hemoglobin. One oxygen molecule can bind to the ferrous iron of a heme molecule in each of the four chains of a hemoglobin molecule.
The first description of cooperative binding to a multi-site protein was developed by A.V. Hill. [4] Drawing on observations of oxygen binding to hemoglobin and the idea that cooperativity arose from the aggregation of hemoglobin molecules, each one binding one oxygen molecule, Hill suggested a phenomenological equation that has since been named after him:
The Root effect is a physiological phenomenon that occurs in fish hemoglobin, named after its discoverer R. W. Root.It is the phenomenon where an increased proton or carbon dioxide concentration (lower pH) lowers hemoglobin's affinity and carrying capacity for oxygen.