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Updated: Jul 13, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
Heme binding to albuminoid proteins is the result of recent evolution
Mauro Fasano1, Gabriella Fanali, Loris Leboffe
1Dipartimento di Biologia Strutturale e Funzionale, and Centro di Neuroscienze, Università dell'Insubria, Busto Arsizio, VA, Italy. mauro.fasano@uninsubria.it
Abstract:
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.
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