Product Code Database
Biliverdin (from the Latin for green bile) is a green tetrapyrrolic bile pigment, and is a product of heme catabolism.Boron W, Boulpaep E. Medical Physiology: a cellular and molecular approach, 2005. 984–986. Elsevier Saunders, United States. It is the pigment responsible for a greenish color sometimes seen in .
Biliverdin is seen briefly in some bruises as a green color. In bruises, its breakdown into bilirubin leads to a yellowish color.
Bile pigments such as biliverdin possess significant anti-mutagenic and antioxidant properties and therefore, may fulfil a useful physiological function. Biliverdin and bilirubin have been shown to be potent scavengers of Hydroperoxyl. They have also been shown to inhibit the effects of polycyclic aromatic hydrocarbons, heterocyclic amines, and – all of which are . Some studies have found that people with higher concentration levels of bilirubin and biliverdin in their bodies have a lower frequency of cancer and cardiovascular disease. It has been suggested that biliverdin – as well as many other tetrapyrrolic pigments – may function as an HIV-1 protease inhibitor as well as having beneficial effects in asthma though further research is needed to confirm these results. There are currently no practical implications for using biliverdin in the treatment of any disease.
Research has shown that the biliverdin of egg shells is produced from the shell gland, rather than from the breakdown of erythrocytes in the blood stream, although there is no evidence that the sources of the material are neither nor free haem from the blood plasma.
Along with its presence in avian egg shells, other studies have also shown that biliverdin is present in the blue-green blood of many marine fish, the blood of tobacco hornworm, the wings of moth and butterfly, the serum and eggs of frogs, and the placenta of dogs. With dogs this can lead, in extremely rare cases, to the birth of puppies with green fur; however, the green color fades out soon after birth. In the garfish ( Belone belone) and related species, the bones are bright green because of biliverdin. The green coloration of many grasshoppers and lepidopteran larvae is also due to biliverdin.
Biliverdin is also present in the green blood, muscles, bones, and mucosal lining of skinks of the genus Prasinohaema, found in New Guinea. It is uncertain whether this presence of biliverdin is an ecological or physiological adaptation of any kind. It has been suggested that accumulation of biliverdin might deter harmful infection by Plasmodium malaria parasites, although no statistically significant correlation has been established. The Cambodian frog, Chiromantis samkosensis, also exhibits this characteristic along with turquoise bones.
A new class of fluorescent protein was evolved from a ( Trichodesmium erythraeum) phycobiliprotein, α-allophycocyanin, and named small ultra red fluorescent protein (smURFP) in 2016. smURFP Catalysis self-incorporates the chromophore biliverdin without the need of an external protein, known as a lyase. Jellyfish- and coral-derived fluorescent proteins require oxygen and produce a Stoichiometry amount of hydrogen peroxide upon chromophore formation. smURFP does not require oxygen or produce hydrogen peroxide and uses the chromophore biliverdin. smURFP has a large extinction coefficient (180,000 M−1 cm−1) and has a modest quantum yield (0.20), which makes it comparable biophysical brightness to eGFP and about 2-fold brighter than most red or far-red fluorescent proteins derived from coral. smURFP spectral properties are similar to the organic dye Cy5.
|
|
