Human α-fetoprotein as a Zn²⁺-binding Protein. Tight Cation Binding is Not Accompanied by Global Changes in Protein Structure and Stability

Authors

Sergei E. Permyakov, Institute for Biological Instrumentation of the Russian Academy of Sciences
Keith A. Oberg, University of California, Santa Cruz
Alexandra M. Cherskaya, Institute for Biological Instrumentation of the Russian Academy of Sciences
Michail M. Shavlovsky, Institute of Cytology of the Russian Academy of Sciences
Eugene A. Permyakov, Institute for Biological Instrumentation of the Russian Academy of Sciences
Vladimir N. Uversky, Institute for Biological Instrumentation of the Russian Academy of SciencesFollow

Document Type

Article

Publication Date

2002

Keywords

α-fetoprotein, Carcinoembryonic Protein, Protein Structure Structural Transition, Conformational Stability, Zn2+ Binding

Digital Object Identifier (DOI)

https://doi.org/10.1016/S0925-4439(01)00079-5

Abstract

The binding of zinc to human α-fetoprotein (AFP) isolated from human umbilical cord serum was studied by fluorimetric Zn2+-titration. We found that the total number of strong binding sites for zinc on this protein was 5: AFP has one very strong (dissociation constant, KdKd

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, v. 1586, issue 1, p. 1-10

Scholar Commons Citation

Permyakov, Sergei E.; Oberg, Keith A.; Cherskaya, Alexandra M.; Shavlovsky, Michail M.; Permyakov, Eugene A.; and Uversky, Vladimir N., "Human α-fetoprotein as a Zn²⁺-binding Protein. Tight Cation Binding is Not Accompanied by Global Changes in Protein Structure and Stability" (2002). Molecular Medicine Faculty Publications. 682.
https://digitalcommons.usf.edu/mme_facpub/682