Journal
PROTEIN AND PEPTIDE LETTERS
Volume 12, Issue 1, Pages 75-+Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/0929866053405931
Keywords
human neuronal tau; 8-anilino-l-naphthalenesulfonic acid (ANS); tau aggregation; denaturation; formaldehyde
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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-anilino1-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.
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