Structural properties of alpha-fetoprotein from human cord serum: the protein molecule at low pH possesses all the properties of the molten globule

FEBS Letters
V N Uversky Tomashevski AYu

Abstract

Structural studies of alpha-fetoprotein (AFP) from human cord serum have shown that a decrease in pH to 3.1 leads to a considerable conformational rearrangement of the protein molecule. The acid form of AFP belongs to the class of denatured conformations and fulfills all the requirements of the molten globule state. The possible functional role of such a transformation is discussed.

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Citations

Jun 15, 2013·Tumour Biology : the Journal of the International Society for Oncodevelopmental Biology and Medicine·A A Terentiev, N T Moldogazieva
Sep 27, 2000·Biochimica Et Biophysica Acta·J R Gillespie, V N Uversky
Jan 27, 2007·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Patrizia CarliniGiuseppe Rotilio
Oct 31, 2009·International Journal of Biological Macromolecules·Peng QuZuhong Lu
Jun 30, 1997·FEBS Letters·V N Uversky Tomashevski AYu
Apr 29, 1995·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·O B PtitsynV N Uversky
Nov 16, 2005·Proteins·Véronique Receveur-BréchotSonia Longhi
Oct 31, 2014·The Journal of Immunology : Official Journal of the American Association of Immunologists·Angela D PardeeLisa H Butterfield
Nov 13, 1998·Journal of Virology·M D KirkitadzeD A McClelland

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