hemocyanin


Also found in: Medical, Encyclopedia, Wikipedia.
Related to hemocyanin: Hemerythrin

he·mo·cy·a·nin

 (hē′mō-sī′ə-nĭn)
n.
A bluish, copper-containing protein with an oxygen-carrying function similar to that of hemoglobin, present in the circulatory system of certain mollusks and arthropods.

he•mo•cy•a•nin

(ˌhi məˈsaɪ ə nɪn)

n.
a blue copper-containing pigment that transports oxygen in the blood of many mollusks, crustaceans, and other invertebrates.
[1835–45; hemo- + Greek kýan(os) (see cyano-1) + -in1]
Mentioned in ?
References in periodicals archive ?
(2013) found changes in the bled horseshoe crab's activity levels, expression of circatidal rhythms, linear and angular movement velocities, and hemocyanin levels.
(Interesting fact: horseshoe crabs use hemocyanin to carry oxygen through their blood.
Stellar Biotechnologies Inc is the leader in sustainable manufacture of Keyhole Limpet Hemocyanin (KLH), an immune-stimulating protein utilized as a carrier molecule in therapeutic vaccine pipelines (targeting cancers, immune disorders, Alzheimer's and inflammatory diseases) and for assessing immune system function.
Animals are vaccinated with a model antigen such as keyhole limpet hemocyanin (KLH) and the resulting antigen-specific antibody production is measured.
The conversion of pigments responsible for the transport of oxygen, such as hemocyanin, in forms incapable of carrying out transportation (metahemocyanin) is the main toxic action of nitrate in aquatic animals, reducing the availability of oxygen for metabolism and may induce hypoxia and mortality (CHENG & CHEN, 2002; JENSEN, 1996; SCOTT & CRUNKILTON, 2000; TAHON et al., 1988).
An additional aim of the study was to document for the first time the major contributing peptide sequence of hemocyanin subunit 2, an immune-related protein, during stress associated with eyestalk ablation in female M.
In spiders, oxygen is bound to hemocyanin, a molecule that contains copper rather than iron.
One week following the last injection, mice were immunized in the footpad with 100 [micro]g/mouse of Keyhole limpet hemocyanin (KLH) (Calbiochem) in Alum (Pierce) weekly for two weeks.
The high degree of oligomerization of hemocyanin molecules, in general, is probably one of the reasons for their increased thermal stability.
The nitrite binds to hemocyanin, occupying the active site in place of oxygen and causing a transformation to meta-hemocyanin, which is unable to transfer oxygen to the tissues.