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Formation of a new fluorescence of human neuronal tau protein

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Chinese Science Bulletin

Abstract

A new fluorescence at 333 nm formed when the solution of human neuronal tau protein was incubated at 37°C. The maximum excitation was at 230 and 280 nm respectively with the quantum yield of about 0.02. It took about 30 h for the complete formation of the new fluorescence and the light scattering increased with the formation procedure. It suggests that the fluorescence resulted from the aggregation of tau molecules in solution.

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References

  1. Goedert, M., Jakes, R., Spillantini, M. G.et al., Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans,Nature, 1996, 383: 550.

    Article  Google Scholar 

  2. Goedert, M., Baur, C. P., Ahringer, J.et al., PTL-1, a microtubule-associated protein with tau-like repeats from the nematode Caenorhabditis elegans,J. Cell. Science, 1996, 109: 2661.

    Google Scholar 

  3. Goedert, M., Tau protein and the neurofibrillary pathology of Alzheimer’s disease,TINS. 1993, 16: 460.

    Google Scholar 

  4. Schweers, O., Schonbrum-Hanebeck, E., Marx, A.et al., Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for β-structure,Journal of Biological Chemistry, 1994, 269: 24290.

    Google Scholar 

  5. Goedert, M., Spillantini, M. G., Potier, M. C.et al., Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain,EMBO Journal, 1989, 8: 393.

    Google Scholar 

  6. Teale, F. F., Weber, G., Ultraviolet fluorescence of aromatic amino acids,Biochem. J., 1957, 65: 476.

    Google Scholar 

  7. Scott, G., Spencer, R. D., Leonard, V. J.et al., Emission properties of NADH. Studies of fluorescence lifetimes and quantum efficiencies of NADH, AcPyADH and simplified synthetic models,Amer. Chew. Soc., 1970, 92: 687.

    Article  Google Scholar 

  8. Mar, P., José, M. V., Miguel, M.et al., Polymerization of τ into filaments in the presence of heparin: the minimal sequence required for τ-τ interaction,Journal of Neuro-chemistry, 1996, 67: 1183.

    Google Scholar 

  9. He, R. Q., Tsou, C. L., Fluorescence of peptide N-terminal 2-oxoacyl and quino derivatives,The Biochemical Journal, 1992, 287: 1001.

    Google Scholar 

  10. He, R. Q., Yang, M. D., Zeng, X.et al., Isolation and some properties of glycated D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle,Biochem. J., 1995, 309: 133.

    Google Scholar 

  11. He, R. Q., Zhao, K. Y., Yan, Z. Z.et al., D-glyceraldehyde-3-phosphate dehydrogenase and maltotetraose-forming amylase from an Alcaligenes sp. during guanidine denaturation,Biochim. Biophysi. Acta., 1993, 1163: 315.

    Google Scholar 

  12. He, R. Q., Li, Y. G., Wu, X. Q.et al., D-glyceraldehyde-3-phosphate dehydrogenase during guanidine-HCl denaturation,Biochim. Biophysi. Acta., 1995, 1253: 47.

    Google Scholar 

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Luo, J., Li, W. & He, R. Formation of a new fluorescence of human neuronal tau protein. Chin.Sci.Bull. 44, 233–236 (1999). https://doi.org/10.1007/BF02896281

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  • DOI: https://doi.org/10.1007/BF02896281

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