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