Structural Properties of α-fetoprotein from Human Cord Serum: the Protein Molecule at Low Ph Possesses All the Properties of the Molten Globule

Authors

Vladimir N. Uversky, Institute of Protein Research of the Russian Academy of SciencesFollow
Marina D. Kirkitadze, Institute of Protein Research of the Russian Academy of Sciences
Natalya V. Narizhneva, Institute of Protein Research of the Russian Academy of Sciences
Sergey A. Potekhin, Institute of Protein Research of the Russian Academy of Sciences
Andrey Yu. Tomashevsky, Institute of Biochemistry and Physiology of Microorganisms

Document Type

Article

Publication Date

1995

Digital Object Identifier (DOI)

https://doi.org/10.1016/0014-5793(95)00379-N

Abstract

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.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

FEBS Letters, v. 364, issue 2, p. 165-167

Scholar Commons Citation

Uversky, Vladimir N.; Kirkitadze, Marina D.; Narizhneva, Natalya V.; Potekhin, Sergey A.; and Tomashevsky, Andrey Yu., "Structural Properties of α-fetoprotein from Human Cord Serum: the Protein Molecule at Low Ph Possesses All the Properties of the Molten Globule" (1995). Molecular Medicine Faculty Publications. 632.
https://digitalcommons.usf.edu/mme_facpub/632