Scientists have often wondered how woolly mammoths survived and thrived in the frigid climes of the far north in Earth’s last ice age. The hemoglobin in elephant (and human) blood cannot easily transfer oxygen to other cells in the body at low temperatures. Instead, the blood’s hemoglobin holds onto its oxygen in icy extremities and the tissue eventually dies; that’s the main reason we get frostbite. There must, then, have been something special about mammoth hemoglobin.
Enter researcher Kevin Campbell, who published the genetic code of the mammoth hemoglobin last year after taking tissue from three animals that died in Siberia more than 25,000 years ago. Now, in a new study in the journal Biochemistry, Campbell’s team went a step further and actually recreated mammoth hemoglobin, starting with the code from the African elephant’s protein and introducing three changes unique to the mammoth using site-directed mutagenesis. They then compared the biochemical properties of the protein from the mammoth, elephant, and human, and found that the mammoth hemoglobin was less sensitive to temperature fluctuations and better able to unload oxygen at cold temperatures. Researchers say insights into the compound’s structure could lead to the design of new artificial blood products for use in hypothermia induced during brain and heart surgeries.
[Via Scientific American]
Reference: Yue Yuan, Tong-Jian Shen, Priyamvada Gupta, Nancy T. Ho, Virgil Simplaceanu, Tsuey Chyi S. Tam, Michael Hofreiter, Alan Cooper, Kevin L. Campbell, Chien Ho. A Biochemical–Biophysical Study of Hemoglobins from Woolly Mammoth, Asian Elephant, and Humans. Biochemistry, 2011; 50 (34): 7350 DOI: 10.1021/bi200777j
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