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

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

Structural studies of α-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 g...

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Veröffentlicht in:FEBS letters 1995-05, Vol.364 (2), p.165-167
Hauptverfasser: Uversky, Vladimir N., Kirkitadze, Marina D., Narizhneva, Natalya V., Potekhin, Sergey A., Tomashevski, Andrey Yu
Format: Artikel
Sprache:eng
Schlagworte:
alpha-Fetoproteins - chemistry
alpha-Fetoproteins - metabolism
Anilino Naphthalenesulfonates - metabolism
Circular dichroism
Fetal Blood - chemistry
Humans
Hydrogen-Ion Concentration
In Vitro Techniques
Infant, Newborn
Molecular Structure
Protein Conformation
Protein Denaturation
Protein stability
Protein Structure, Tertiary
Scanning microcalorimetry
Thermodynamics
α-Fetoprotein
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Zusammenfassung:Structural studies of α-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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00379-N