Journal of Applied Biological Chemistry

The Korean Society for Applied Biological Chemistry (한국응용생명화학회)
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Effects of heavy metals and albumin on lysozyme activity

  • Ko, Eun (Department of Bioengineering and Biotechnology, College of Engineering, Chonnam National University) ;
  • Ku, Seul-I (Interdisciplinary Program of Bioenergy and Biomaterials Graduate School (BK21 Plus Program), College of Engineering, Chonnam National University) ;
  • Kim, Dae-yoon (Department of Optometry, College of Energy and Biotechnology, Seoul National University of Science and Technology) ;
  • Shin, Sooim (Interdisciplinary Program of Bioenergy and Biomaterials Graduate School (BK21 Plus Program), College of Engineering, Chonnam National University) ;
  • Choi, Moonsung (Department of Optometry, College of Energy and Biotechnology, Seoul National University of Science and Technology)
  • Received : 2018.09.07
  • Accepted : 2018.10.31
  • Published : 2018.12.31
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Abstract

Lysozyme is an antibacterial enzyme that is found in most of body fluids. Lysozyme in tears plays a primary role in protecting eye from harmful environments; if lysozyme is degraded or inhibited, eyes are likely to be more vulnerable to bacterial infection. In this study, lysozyme activity was evaluated according to varying concentrations of heavy metals, copper, zinc, cobalt and manganese and light metal, calcium that are frequently found in airborne particulate matters and was assayed using a dye-quenching lysozyme substrate, Micrococcus lysodeikticus. Less fluorescence intensity was observed with increasing amounts of copper, zinc, manganese and cobalt but not with calcium suggesting that these metals have some affinity with lysozyme and inhibit lysozyme activity. When albumin, the second most common protein in tears, was added on the reaction of lysozyme and metals, lysozyme activity was partially restored. This finding suggests that the albumin might protect damage caused by metals on lysozyme. To identify whether the decrease in enzymatic activity was related to structural changes of lysozyme, SDS-PAGE was conducted and only with copper did lysozyme show marked smearing bands on the SDS-gel, meaning that copper degraded lysozyme consistent with the sharpest activity decrease.

Keywords

References

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