Novel way to remove iron from ferritin discoveredNovember 14th, 2007 - 8:24 am ICT by admin
The scientists knew that the ferritin protein cage had pores that could open and close. They also knew that chelators, a method to detoxify blood, removed iron faster when the pores were open.
“We wanted to prove a hypothesis that a small protein or peptide could bind to ferritin and could be used to regulate ferritin pores,” said Dr. Elizabeth Theil of Children’s Hospital Oakland Research Institute, who authored the report.
“Our hypothesis was correct. We proved that when a binding peptide of seven amino acids, a heptapeptide, is coupled with Desferal the rate of removal of iron from ferritin is eight times faster,” she added.
The findings are the result of a study that Dr. Theil conducted in collaboration with researchers from the University of Notre Dame.
The researchers have described their work in the Journal of Biological Chemistry. (ANI)
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Tags: concentrates, desferal, detoxify, dr elizabeth, eight times, ferritin, hospital oakland, hypothesis, inner core, journal of biological chemistry, peptide, pores, protein cage, s hospital, theil, university of notre dame