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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Heme binding to albuminoid proteins is the result of recent evolution.

We hypothesize that the structure of the heme binding site of paralogous albuminoids alpha-fetoprotein and serum albumin has evolved from the ancestor vitamin D binding protein through the 'phylogenetic intermediate' afamin, the most recently discovered albuminoid. Heme binding to plasma proteins should serve not only as a buffer for heme homeostasis, avoiding heme binding to lipoproteins with the consequent oxidative stress, but also for heme transfer to the liver, complementing the function of hemopexin.[1]

References

  1. Heme binding to albuminoid proteins is the result of recent evolution. Fasano, M., Fanali, G., Leboffe, L., Ascenzi, P. IUBMB. Life (2007) [Pubmed]
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