Changes in conformation of human neuronal tau during denaturation in formaldehyde solution.
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.
Nie
Chun-Lai
CL
Lab of Visual Information Processing, Institute of Biophysics, Chinese Academy of Sciences, Beijing.
Zhang
Wei
W
Zhang
Dai
D
He
Rong-Qiao
RQ
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
D000817:Anilino Naphthalenesulfonates; D012996:Solutions; D016875:tau Proteins; D005557:Formaldehyde; C027132:1-anilino-8-naphthalenesulfonate