Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL
USA
Email: bdunn@ufl.edu

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Changes in Conformation of Human Neuronal Tau During Denaturation in Formaldehyde Solution

Author(s): Chun-Lai Nie, Wei Zhang, Dai Zhang and Rong-Qiao He

Affiliation: Institute of Biophysics, Chinese Academy of Sciences, Beijing University, Beijing.

Abstract:

Human neuronal tau was incubated in formaldehyde solution at low concentrations and the intensity of light scattering of tau-40 solution at 480 nm increased markedly. Then potassium iodide was used to quench the intrinsic fluorescence of tau. The fluorescent quenching constants decreased as formaldehyde concentrations increased. 8-anilino- 1-naphthalenesulfonic acid (ANS) binding assay showed that a putative hydrophobic core formed in tau polymers during incubation with formaldehyde. Native tau was hydrolyzed by immobilized earthworm fibrinolytic enzyme-II (EFE-II), producing a digested fragment (36-37 kDa). However, formaldehyde-treated tau could not be digested under the same conditions, suggesting that aggregated protein was relatively rigidly deposited.

Keywords: human neuronal tau, 8-anilino-1-naphthalenesulfonic acid, tau aggregation, denaturation, formaldehyde

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Article Details

VOLUME: 12
ISSUE: 1
Page: [75 - 78]
Pages: 4
DOI: 10.2174/0929866053405931