Abstract
Abstract: α-Fetoprotein samples isolated from human cord serum by different methods were compared using circular dichroism, scanning microcalorimetry and fluorescence spectroscopy. Their structural properties and conformational stability were appreciably discriminated. In particular, the protein molecule had either one or two relatively rigid domains which can be co-operatively disrupted by heating or urea treatment. This is due to the difference of the isolation procedures in their capabilities to strip the natural ligands from the protein molecule.
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