PMID: 6978319Mar 1, 1982Paper

Lysozyme dimer formation on lysozyme oxidation with Br2 radical as studied by fluorescence evolution

International Journal of Radiation Biology and Related Studies in Physics, Chemistry, and Medicine
S HashimotoT Masuda

Abstract

Lysozyme dimers produced on oxidation of lysozyme with Br2 radical in aqueous solutions exhibit a fluorescence spectrum (lambda max = 400 nm) closely similar to that of bi-tyrosine. This suggests that the dimer is likely to have a tyrosine-tyrosine bond resulting from the combination of tyrosine phenoxy radicals of two lysozyme molecules. Kinetic studies on dimer formation were made by measuring time-dependent fluorescence after pulsed-electron irradiation over wide pH range. The results lead to the following conclusions. The second-order growth of the dimer fluorescence observed at pH 10.7-12.5 reflects the combination process of the lysozyme radicals, which is rate-determining in the pH range. On the other hand, the first-order growth observed at pH 6.8-10.2 is attributable to the enolization of the keto-form of the dimer. A tentative reaction scheme is proposed for the dimer formation.

References

Nov 1, 1976·Photochemistry and Photobiology·I TatischeffM Duquesne
Jul 20, 1966·Journal of the American Chemical Society·H I Joschek, S I Miller
Sep 16, 1980·Biochemical and Biophysical Research Communications·W A PrützA J Swallow
Aug 1, 1960·The Biochemical Journal·F W TEALE
Feb 5, 1963·Biochimica Et Biophysica Acta·S O ANDERSEN

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Citations

Dec 7, 1984·Biochimica Et Biophysica Acta·B M Hoey, J Butler

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