title: Changes in conformation of human neuronal tau during denaturation in formaldehyde solution.
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.
authors.affiliation: Lab of Visual Information Processing, Institute of Biophysics, Chinese Academy of Sciences, Beijing.
authors.forename: Chun-Lai
authors.initials: CL
authors.lastname: Nie
authors.forename: Wei
authors.initials: W
authors.lastname: Zhang
authors.forename: Dai
authors.initials: D
authors.lastname: Zhang
authors.forename: Rong-Qiao
authors.initials: RQ
authors.lastname: He
mesh_terms: D000817:Anilino Naphthalenesulfonates / Q000378:metabolism; D005557:Formaldehyde / Q000494:pharmacology*; D006801:Humans; D011487:Protein Conformation; D011489:Protein Denaturation; D012996:Solutions / Q000737:chemistry; D016875:tau Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D000817:Anilino Naphthalenesulfonates; D012996:Solutions; D016875:tau Proteins; D005557:Formaldehyde; C027132:1-anilino-8-naphthalenesulfonate